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PDBsum entry 1asy

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protein dna_rna Protein-protein interface(s) links
Complex (aminoacyl-tRNA synthase/tRNA) PDB id
1asy
Jmol
Contents
Protein chains
490 a.a. *
DNA/RNA
* Residue conservation analysis
PDB id:
1asy
Name: Complex (aminoacyl-tRNA synthase/tRNA)
Title: Class ii aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA asp
Structure: T-RNA (75-mer). Chain: r, s. Engineered: yes. Aspartyl-tRNA synthetase. Chain: a, b. Engineered: yes
Source: Synthetic: yes. Saccharomyces cerevisiae
Biol. unit: Tetramer (from PQS)
Resolution:
2.90Å     R-factor:   0.225    
Authors: M.Ruff,J.Cavarelli,B.Rees,S.Krishnaswamy,J.C.Thierry,D.Moras
Key ref: M.Ruff et al. (1991). Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp). Science, 252, 1682-1689. PubMed id: 2047877 DOI: 10.1126/science.2047877
Date:
19-Jan-95     Release date:   08-May-95    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P04802  (SYDC_YEAST) -  Aspartate--tRNA ligase, cytoplasmic
Seq:
Struc:
 
Seq:
Struc:
557 a.a.
490 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.6.1.1.12  - Aspartate--tRNA ligase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
ATP
+ L-aspartate
+ tRNA(Asp)
= AMP
+ diphosphate
+ L-aspartyl-tRNA(Asp)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     tRNA aminoacylation for protein translation   2 terms 
  Biochemical function     nucleotide binding     5 terms  

 

 
    reference    
 
 
DOI no: 10.1126/science.2047877 Science 252:1682-1689 (1991)
PubMed id: 2047877  
 
 
Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp).
M.Ruff, S.Krishnaswamy, M.Boeglin, A.Poterszman, A.Mitschler, A.Podjarny, B.Rees, J.C.Thierry, D.Moras.
 
  ABSTRACT  
 
The crystal structure of the binary complex tRNA(Asp)-aspartyl tRNA synthetase from yeast was solved with the use of multiple isomorphous replacement to 3 angstrom resolution. The dimeric synthetase, a member of class II aminoacyl tRNA synthetases (aaRS's) exhibits the characteristic signature motifs conserved in eight aaRS's. These three sequence motifs are contained in the catalytic site domain, built around an antiparallel beta sheet, and flanked by three alpha helices that form the pocket in which adenosine triphosphate (ATP) and the CCA end of tRNA bind. The tRNA(Asp) molecule approaches the synthetase from the variable loop side. The two major contact areas are with the acceptor end and the anticodon stem and loop. In both sites the protein interacts with the tRNA from the major groove side. The correlation between aaRS class II and the initial site of aminoacylation at 3'-OH can be explained by the structure. The molecular association leads to the following features: (i) the backbone of the GCCA single-stranded portion of the acceptor end exhibits a regular helical conformation; (ii) the loop between residues 320 and 342 in motif 2 interacts with the acceptor stem in the major groove and is in contact with the discriminator base G and the first base pair UA; and (iii) the anticodon loop undergoes a large conformational change in order to bind the protein. The conformation of the tRNA molecule in the complex is dictated more by the interaction with the protein than by its own sequence.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19906721 A.Nakamura, K.Sheppard, J.Yamane, M.Yao, D.Söll, and I.Tanaka (2010).
Two distinct regions in Staphylococcus aureus GatCAB guarantee accurate tRNA recognition.
  Nucleic Acids Res, 38, 672-682.
PDB code: 3ip4
20498460 C.E.Hajdin, F.Ding, N.V.Dokholyan, and K.M.Weeks (2010).
On the significance of an RNA tertiary structure prediction.
  RNA, 16, 1340-1349.  
19874856 E.A.Merritt, T.L.Arakaki, E.T.Larson, A.Kelley, N.Mueller, A.J.Napuli, L.Zhang, G.Deditta, J.Luft, C.L.Verlinde, E.Fan, F.Zucker, F.S.Buckner, W.C.Van Voorhis, and W.G.Hol (2010).
Crystal structure of the aspartyl-tRNA synthetase from Entamoeba histolytica.
  Mol Biochem Parasitol, 169, 95.
PDB code: 3i7f
20717102 M.Blaise, M.Bailly, M.Frechin, M.A.Behrens, F.Fischer, C.L.Oliveira, H.D.Becker, J.S.Pedersen, S.Thirup, and D.Kern (2010).
Crystal structure of a transfer-ribonucleoprotein particle that promotes asparagine formation.
  EMBO J, 29, 3118-3129.
PDB code: 3kfu
21119764 R.Giegé, and C.Sauter (2010).
Biocrystallography: past, present, future.
  HFSP J, 4, 109-121.  
20882017 T.Ito, and S.Yokoyama (2010).
Two enzymes bound to one transfer RNA assume alternative conformations for consecutive reactions.
  Nature, 467, 612-616.
PDB codes: 3akz 3al0
  19555498 D.Vlachakis (2009).
Theoretical study of the Usutu virus helicase 3D structure, by means of computer-aided homology modelling.
  Theor Biol Med Model, 6, 9.  
19118381 K.Nozawa, P.O'Donoghue, S.Gundllapalli, Y.Araiso, R.Ishitani, T.Umehara, D.Söll, and O.Nureki (2009).
Pyrrolysyl-tRNA synthetase-tRNA(Pyl) structure reveals the molecular basis of orthogonality.
  Nature, 457, 1163-1167.
PDB codes: 2zni 2znj
19767615 M.Messmer, J.Pütz, T.Suzuki, T.Suzuki, C.Sauter, M.Sissler, and F.Catherine (2009).
Tertiary network in mammalian mitochondrial tRNAAsp revealed by solution probing and phylogeny.
  Nucleic Acids Res, 37, 6881-6895.  
19443655 T.Bour, A.Akaddar, B.Lorber, S.Blais, C.Balg, E.Candolfi, and M.Frugier (2009).
Plasmodial aspartyl-tRNA synthetases and peculiarities in Plasmodium falciparum.
  J Biol Chem, 284, 18893-18903.  
18755841 C.M.Zhang, C.Liu, T.Christian, H.Gamper, J.Rozenski, D.Pan, J.B.Randolph, E.Wickstrom, B.S.Cooperman, and Y.M.Hou (2008).
Pyrrolo-C as a molecular probe for monitoring conformations of the tRNA 3' end.
  RNA, 14, 2245-2253.  
18076053 D.Thompson, C.Lazennec, P.Plateau, and T.Simonson (2008).
Probing electrostatic interactions and ligand binding in aspartyl-tRNA synthetase through site-directed mutagenesis and computer simulations.
  Proteins, 71, 1450-1460.  
18548004 H.Xiao, H.Murakami, H.Suga, and A.R.Ferré-D'Amaré (2008).
Structural basis of specific tRNA aminoacylation by a small in vitro selected ribozyme.
  Nature, 454, 358-361.
PDB codes: 3cul 3cun
18172502 K.Beebe, M.Mock, E.Merriman, and P.Schimmel (2008).
Distinct domains of tRNA synthetase recognize the same base pair.
  Nature, 451, 90-93.  
18272479 M.Guo, M.Ignatov, K.Musier-Forsyth, P.Schimmel, and X.L.Yang (2008).
Crystal structure of tetrameric form of human lysyl-tRNA synthetase: Implications for multisynthetase complex formation.
  Proc Natl Acad Sci U S A, 105, 2331-2336.
PDB code: 3bju
18384044 S.Goto-Ito, T.Ito, R.Ishii, Y.Muto, Y.Bessho, and S.Yokoyama (2008).
Crystal structure of archaeal tRNA(m(1)G37)methyltransferase aTrm5.
  Proteins, 72, 1274-1289.
PDB code: 2yx1
18322459 S.N.Rodin, and A.S.Rodin (2008).
On the origin of the genetic code: signatures of its primordial complementarity in tRNAs and aminoacyl-tRNA synthetases.
  Heredity, 100, 341-355.  
18573090 S.R.Holbrook (2008).
Structural principles from large RNAs.
  Annu Rev Biophys, 37, 445-464.  
18716674 S.Shazman, and Y.Mandel-Gutfreund (2008).
Classifying RNA-binding proteins based on electrostatic properties.
  PLoS Comput Biol, 4, e1000146.  
19022179 T.Yanagisawa, R.Ishii, R.Fukunaga, T.Kobayashi, K.Sakamoto, and S.Yokoyama (2008).
Multistep engineering of pyrrolysyl-tRNA synthetase to genetically encode N(epsilon)-(o-azidobenzyloxycarbonyl) lysine for site-specific protein modification.
  Chem Biol, 15, 1187-1197.
PDB codes: 2zin 2zio
17704131 E.Jakó, P.Ittzés, A.Szenes, A.Kun, E.Szathmáry, and G.Pál (2007).
In silico detection of tRNA sequence features characteristic to aminoacyl-tRNA synthetase class membership.
  Nucleic Acids Res, 35, 5593-5609.  
17447878 I.A.Vasil'eva, and N.A.Moor (2007).
Interaction of aminoacyl-tRNA synthetases with tRNA: general principles and distinguishing characteristics of the high-molecular-weight substrate recognition.
  Biochemistry (Mosc), 72, 247-263.  
  17620724 K.Suzuki, Y.Sato, Y.Maeda, S.Shimizu, M.T.Hossain, S.Ubukata, T.Sekiguchi, and A.Takénaka (2007).
Crystallization and preliminary X-ray crystallographic study of a putative aspartyl-tRNA synthetase from the crenarchaeon Sulfolobus tokodaii strain 7.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 608-612.  
17386262 Y.Pham, L.Li, A.Kim, O.Erdogan, V.Weinreb, G.L.Butterfoss, B.Kuhlman, and C.W.Carter (2007).
A minimal TrpRS catalytic domain supports sense/antisense ancestry of class I and II aminoacyl-tRNA synthetases.
  Mol Cell, 25, 851-862.  
17881821 Y.Sato, Y.Maeda, S.Shimizu, M.T.Hossain, S.Ubukata, K.Suzuki, T.Sekiguchi, and A.Takénaka (2007).
Structure of the nondiscriminating aspartyl-tRNA synthetase from the crenarchaeon Sulfolobus tokodaii strain 7 reveals the recognition mechanism for two different tRNA anticodons.
  Acta Crystallogr D Biol Crystallogr, 63, 1042-1047.
PDB code: 1wyd
16636827 M.V.Petoukhov, and D.I.Svergun (2006).
Joint use of small-angle X-ray and neutron scattering to study biological macromolecules in solution.
  Eur Biophys J, 35, 567-576.  
16798914 N.Shen, L.Guo, B.Yang, Y.Jin, and J.Ding (2006).
Structure of human tryptophanyl-tRNA synthetase in complex with tRNATrp reveals the molecular basis of tRNA recognition and specificity.
  Nucleic Acids Res, 34, 3246-3258.
PDB codes: 2ake 2dr2
17206068 R.Giegé (2006).
The early history of tRNA recognition by aminoacyl-tRNA synthetases.
  J Biosci, 31, 477-488.  
16645791 S.C.Sukuru, T.Crepin, Y.Milev, L.C.Marsh, J.B.Hill, R.J.Anderson, J.C.Morris, A.Rohatgi, G.O'Mahony, M.Grøtli, F.Danel, M.G.Page, M.Härtlein, S.Cusack, M.A.Kron, and L.A.Kuhn (2006).
Discovering new classes of Brugia malayi asparaginyl-tRNA synthetase inhibitors and relating specificity to conformational change.
  J Comput Aided Mol Des, 20, 159-178.  
  17012805 T.Yanagisawa, R.Ishii, R.Fukunaga, O.Nureki, and S.Yokoyama (2006).
Crystallization and preliminary X-ray crystallographic analysis of the catalytic domain of pyrrolysyl-tRNA synthetase from the methanogenic archaeon Methanosarcina mazei.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 1031-1033.  
16153175 A.G.Hinnebusch (2005).
Translational regulation of GCN4 and the general amino acid control of yeast.
  Annu Rev Microbiol, 59, 407-450.  
15755955 B.S.Laursen, H.P.Sørensen, K.K.Mortensen, and H.U.Sperling-Petersen (2005).
Initiation of protein synthesis in bacteria.
  Microbiol Mol Biol Rev, 69, 101-123.  
16113655 M.Frugier, M.Ryckelynck, and R.Giegé (2005).
tRNA-balanced expression of a eukaryal aminoacyl-tRNA synthetase by an mRNA-mediated pathway.
  EMBO Rep, 6, 860-865.  
16155584 R.Fukunaga, and S.Yokoyama (2005).
Aminoacylation complex structures of leucyl-tRNA synthetase and tRNALeu reveal two modes of discriminator-base recognition.
  Nat Struct Mol Biol, 12, 915-922.  
15766524 T.T.Lee, S.Agarwalla, and R.M.Stroud (2005).
A unique RNA Fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function.
  Cell, 120, 599-611.
PDB code: 2bh2
15853794 Y.Chen, and G.Varani (2005).
Protein families and RNA recognition.
  FEBS J, 272, 2088-2097.  
15452274 A.Fender, R.Geslain, G.Eriani, R.Giegé, M.Sissler, and C.Florentz (2004).
A yeast arginine specific tRNA is a remnant aspartate acceptor.
  Nucleic Acids Res, 32, 5076-5086.  
14729701 G.Jäger, R.Leipuviene, M.G.Pollard, Q.Qian, and G.R.Björk (2004).
The conserved Cys-X1-X2-Cys motif present in the TtcA protein is required for the thiolation of cytidine in position 32 of tRNA from Salmonella enterica serovar Typhimurium.
  J Bacteriol, 186, 750-757.  
14757836 J.Liu, E.Shue, K.L.Ewalt, and P.Schimmel (2004).
A new gamma-interferon-inducible promoter and splice variants of an anti-angiogenic human tRNA synthetase.
  Nucleic Acids Res, 32, 719-727.  
15333921 L.Urzhumtseva, N.Lunina, A.Fokine, J.P.Samama, V.Y.Lunin, and A.Urzhumtsev (2004).
Ab initio phasing based on topological restraints: automated determination of the space group and the number of molecules in the unit cell.
  Acta Crystallogr D Biol Crystallogr, 60, 1519-1526.  
15100439 M.Sissler, M.Helm, M.Frugier, R.Giege, and C.Florentz (2004).
Aminoacylation properties of pathology-related human mitochondrial tRNA(Lys) variants.
  RNA, 10, 841-853.  
12777801 A.Fokine, N.Lunina, V.Lunin, and A.Urzhumtsev (2003).
Connectivity-based ab initio phasing at different solvent levels.
  Acta Crystallogr D Biol Crystallogr, 59, 850-858.  
12660169 C.Charron, H.Roy, M.Blaise, R.Giegé, and D.Kern (2003).
Non-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domain.
  EMBO J, 22, 1632-1643.
PDB code: 1n9w
12598368 D.L.Theobald, R.M.Mitton-Fry, and D.S.Wuttke (2003).
Nucleic acid recognition by OB-fold proteins.
  Annu Rev Biophys Biomol Struct, 32, 115-133.  
12754495 T.Kobayashi, O.Nureki, R.Ishitani, A.Yaremchuk, M.Tukalo, S.Cusack, K.Sakamoto, and S.Yokoyama (2003).
Structural basis for orthogonal tRNA specificities of tyrosyl-tRNA synthetases for genetic code expansion.
  Nat Struct Biol, 10, 425-432.
PDB code: 1j1u
12949492 W.Xie, X.Liu, and R.H.Huang (2003).
Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate.
  Nat Struct Biol, 10, 781-788.
PDB codes: 1q2r 1q2s
11983895 A.D.Wolfson, and O.C.Uhlenbeck (2002).
Modulation of tRNAAla identity by inorganic pyrophosphatase.
  Proc Natl Acad Sci U S A, 99, 5965-5970.  
12112691 A.Teplyakov, G.Obmolova, M.Tordova, N.Thanki, N.Bonander, E.Eisenstein, A.J.Howard, and G.L.Gilliland (2002).
Crystal structure of the YjeE protein from Haemophilus influenzae: a putative Atpase involved in cell wall synthesis.
  Proteins, 48, 220-226.
PDB codes: 1fl9 1htw
12110594 A.Yaremchuk, I.Kriklivyi, M.Tukalo, and S.Cusack (2002).
Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition.
  EMBO J, 21, 3829-3840.
PDB codes: 1h3e 1h3f
12087168 C.Mayer, and U.L.RajBhandary (2002).
Conformational change of Escherichia coli initiator methionyl-tRNA(fMet) upon binding to methionyl-tRNA formyl transferase.
  Nucleic Acids Res, 30, 2844-2850.  
12080340 D.Desveaux, J.Allard, N.Brisson, and J.Sygusch (2002).
A new family of plant transcription factors displays a novel ssDNA-binding surface.
  Nat Struct Biol, 9, 512-517.
PDB code: 1l3a
11698642 A.Shimada, O.Nureki, M.Goto, S.Takahashi, and S.Yokoyama (2001).
Structural and mutational studies of the recognition of the arginine tRNA-specific major identity element, A20, by arginyl-tRNA synthetase.
  Proc Natl Acad Sci U S A, 98, 13537-13542.
PDB codes: 1iq0 1ir4
11170439 J.F.Chen, T.Li, E.D.Wang, and Y.L.Wang (2001).
Effect of alanine-293 replacement on the activity, ATP binding, and editing of Escherichia coli leucyl-tRNA synthetase.
  Biochemistry, 40, 1144-1149.  
11223940 J.M.O'Sullivan, M.J.Mihr, M.A.Santos, and M.F.Tuite (2001).
Seryl-tRNA synthetase is not responsible for the evolution of CUG codon reassignment in Candida albicans.
  Yeast, 18, 313-322.  
11297441 K.J.Hampel, and J.M.Burke (2001).
A conformational change in the "loop E-like" motif of the hairpin ribozyme is coincidental with domain docking and is essential for catalysis.
  Biochemistry, 40, 3723-3729.  
11566892 L.Moulinier, S.Eiler, G.Eriani, J.Gangloff, J.C.Thierry, K.Gabriel, W.H.McClain, and D.Moras (2001).
The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism.
  EMBO J, 20, 5290-5301.
PDB code: 1il2
11269237 L.Ribas de Pouplana, and P.Schimmel (2001).
Two classes of tRNA synthetases suggested by sterically compatible dockings on tRNA acceptor stem.
  Cell, 104, 191-193.  
11590011 L.Ribas de Pouplana, and P.Schimmel (2001).
Aminoacyl-tRNA synthetases: potential markers of genetic code development.
  Trends Biochem Sci, 26, 591-596.  
  11375928 M.Ibba, and D.Söll (2001).
The renaissance of aminoacyl-tRNA synthesis.
  EMBO Rep, 2, 382-387.  
11679724 P.Retailleau, Y.Yin, M.Hu, J.Roach, G.Bricogne, C.Vonrhein, P.Roversi, E.Blanc, R.M.Sweet, and C.W.Carter (2001).
High-resolution experimental phases for tryptophanyl-tRNA synthetase (TrpRS) complexed with tryptophanyl-5'AMP.
  Acta Crystallogr D Biol Crystallogr, 57, 1595-1608.
PDB codes: 1i6k 1i6l 1i6m
11679717 R.Fishman, V.Ankilova, N.Moor, and M.Safro (2001).
Structure at 2.6 A resolution of phenylalanyl-tRNA synthetase complexed with phenylalanyl-adenylate in the presence of manganese.
  Acta Crystallogr D Biol Crystallogr, 57, 1534-1544.
PDB code: 1jjc
  11680848 S.T.Nonekowski, and G.A.Garcia (2001).
tRNA recognition by tRNA-guanine transglycosylase from Escherichia coli: the role of U33 in U-G-U sequence recognition.
  RNA, 7, 1432-1441.  
10851193 A.D.Frankel (2000).
Fitting peptides into the RNA world.
  Curr Opin Struct Biol, 10, 332-340.  
11112540 B.Burke, F.Yang, F.Chen, C.Stehlin, B.Chan, and K.Musier-Forsyth (2000).
Evolutionary coadaptation of the motif 2--acceptor stem interaction in the class II prolyl-tRNA synthetase system.
  Biochemistry, 39, 15540-15547.  
10841758 E.Madore, R.S.Lipman, Y.M.Hou, and J.Lapointe (2000).
Evidence for unfolding of the single-stranded GCCA 3'-End of a tRNA on its aminoacyl-tRNA synthetase from a stacked helical to a foldback conformation.
  Biochemistry, 39, 6791-6798.  
10913247 G.Desogus, F.Todone, P.Brick, and S.Onesti (2000).
Active site of lysyl-tRNA synthetase: structural studies of the adenylation reaction.
  Biochemistry, 39, 8418-8425.
PDB codes: 1e1o 1e1t 1e22 1e24
11256617 G.Varani, and W.H.McClain (2000).
The G x U wobble base pair. A fundamental building block of RNA structure crucial to RNA function in diverse biological systems.
  EMBO Rep, 1, 18-23.  
10727213 H.D.Becker, H.Roy, L.Moulinier, M.H.Mazauric, G.Keith, and D.Kern (2000).
Thermus thermophilus contains an eubacterial and an archaebacterial aspartyl-tRNA synthetase.
  Biochemistry, 39, 3216-3230.  
10813833 H.Zhang, K.Huang, Z.Li, L.Banerjei, K.E.Fisher, N.V.Grishin, E.Eisenstein, and O.Herzberg (2000).
Crystal structure of YbaK protein from Haemophilus influenzae (HI1434) at 1.8 A resolution: functional implications.
  Proteins, 40, 86-97.
PDB codes: 1dbu 1dbx
10889033 J.A.Pleiss, A.D.Wolfson, and O.C.Uhlenbeck (2000).
Mapping contacts between Escherichia coli alanyl tRNA synthetase and 2' hydroxyls using a complete tRNA molecule.
  Biochemistry, 39, 8250-8258.  
10983975 J.Dong, H.Qiu, M.Garcia-Barrio, J.Anderson, and A.G.Hinnebusch (2000).
Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain.
  Mol Cell, 6, 269-279.  
10828991 J.F.Chen, N.N.Guo, T.Li, E.D.Wang, and Y.L.Wang (2000).
CP1 domain in Escherichia coli leucyl-tRNA synthetase is crucial for its editing function.
  Biochemistry, 39, 6726-6731.  
11101501 M.A.Swairjo, A.J.Morales, C.C.Wang, A.R.Ortiz, and P.Schimmel (2000).
Crystal structure of trbp111: a structure-specific tRNA-binding protein.
  EMBO J, 19, 6287-6298.
PDB codes: 1pxf 1pyb 3ers
10871402 M.C.Nagan, P.Beuning, K.Musier-Forsyth, and C.J.Cramer (2000).
Importance of discriminator base stacking interactions: molecular dynamics analysis of A73 microhelix(Ala) variants.
  Nucleic Acids Res, 28, 2527-2534.  
10811628 M.Frugier, L.Moulinier, and R.Giegé (2000).
A domain in the N-terminal extension of class IIb eukaryotic aminoacyl-tRNA synthetases is important for tRNA binding.
  EMBO J, 19, 2371-2380.  
10966471 M.Ibba, and D.Soll (2000).
Aminoacyl-tRNA synthesis.
  Annu Rev Biochem, 69, 617-650.  
10694387 S.Gite, Y.Li, V.Ramesh, and U.L.RajBhandary (2000).
Escherichia coli methionyl-tRNA formyltransferase: role of amino acids conserved in the linker region and in the C-terminal domain on the specific recognition of the initiator tRNA.
  Biochemistry, 39, 2218-2226.  
10688361 S.Joseph, M.L.Whirl, D.Kondo, H.F.Noller, and R.B.Altman (2000).
Calculation of the relative geometry of tRNAs in the ribosome from directed hydroxyl-radical probing data.
  RNA, 6, 220-232.  
11041850 S.Onesti, G.Desogus, A.Brevet, J.Chen, P.Plateau, S.Blanquet, and P.Brick (2000).
Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding.
  Biochemistry, 39, 12853-12861.
PDB codes: 1bbu 1bbw
11073219 T.Toyoda, O.F.Tin, K.Ito, T.Fujiwara, T.Kumasaka, M.Yamamoto, M.B.Garber, and Y.Nakamura (2000).
Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as a functional switch.
  RNA, 6, 1432-1444.
PDB code: 1eh1
10449415 A.Bochkarev, E.Bochkareva, L.Frappier, and A.M.Edwards (1999).
The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding.
  EMBO J, 18, 4498-4504.
PDB code: 1quq
10570126 B.A.Steer, and P.Schimmel (1999).
Domain-domain communication in a miniature archaebacterial tRNA synthetase.
  Proc Natl Acad Sci U S A, 96, 13644-13649.  
10213598 B.A.Steer, and P.Schimmel (1999).
Different adaptations of the same peptide motif for tRNA functional contacts by closely homologous tRNA synthetases.
  Biochemistry, 38, 4965-4971.  
10089405 C.Sauter, B.Lorber, D.Kern, J.Cavarelli, D.Moras, and R.Giegé (1999).
Crystallogenesis studies on yeast aspartyl-tRNA synthetase: use of phase diagram to improve crystal quality.
  Acta Crystallogr D Biol Crystallogr, 55, 149-156.  
10387013 J.Horowitz, W.C.Chu, W.B.Derrick, J.C.Liu, M.Liu, and D.Yue (1999).
Synthetase recognition determinants of E. coli valine transfer RNA.
  Biochemistry, 38, 7737-7746.  
10199566 J.Rudinger-Thirion, and R.Giegé (1999).
The peculiar architectural framework of tRNASec is fully recognized by yeast AspRS.
  RNA, 5, 495-502.  
10026283 K.Nadassy, S.J.Wodak, and J.Janin (1999).
Structural features of protein-nucleic acid recognition sites.
  Biochemistry, 38, 1999-2017.  
10385005 L.Jermutus, V.Guez, and H.Bedouelle (1999).
Disordered C-terminal domain of tyrosyl-tRNA synthetase: secondary structure prediction.
  Biochimie, 81, 235-244.  
10213600 M.Fromant, P.Plateau, E.Schmitt, Y.Mechulam, and S.Blanquet (1999).
Receptor site for the 5'-phosphate of elongator tRNAs governs substrate selection by peptidyl-tRNA hydrolase.
  Biochemistry, 38, 4982-4987.  
10737860 P.J.Beuning, and K.Musier-Forsyth (1999).
Transfer RNA recognition by aminoacyl-tRNA synthetases.
  Biopolymers, 52, 1.  
10368282 P.Nissen, S.Thirup, M.Kjeldgaard, and J.Nyborg (1999).
The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA.
  Structure, 7, 143-156.
PDB code: 1b23
10319817 R.Sankaranarayanan, A.C.Dock-Bregeon, P.Romby, J.Caillet, M.Springer, B.Rees, C.Ehresmann, B.Ehresmann, and D.Moras (1999).
The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site.
  Cell, 97, 371-381.
PDB code: 1qf6
10587461 R.W.Alexander, and P.Schimmel (1999).
Evidence for breaking domain-domain functional communication in a synthetase-tRNA complex.
  Biochemistry, 38, 16359-16365.  
10562565 S.Eiler, A.Dock-Bregeon, L.Moulinier, J.C.Thierry, and D.Moras (1999).
Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of the second step.
  EMBO J, 18, 6532-6541.
PDB code: 1c0a
10215844 S.Sekine, O.Nureki, M.Tateno, and S.Yokoyama (1999).
The identity determinants required for the discrimination between tRNAGlu and tRNAAsp by glutamyl-tRNA synthetase from Escherichia coli.
  Eur J Biochem, 261, 354-360.  
10587437 T.M.Larsen, S.K.Boehlein, S.M.Schuster, N.G.Richards, J.B.Thoden, H.M.Holden, and I.Rayment (1999).
Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product.
  Biochemistry, 38, 16146-16157.
PDB code: 1ct9
9582288 C.Berthet-Colominas, L.Seignovert, M.Härtlein, M.Grotli, S.Cusack, and R.Leberman (1998).
The crystal structure of asparaginyl-tRNA synthetase from Thermus thermophilus and its complexes with ATP and asparaginyl-adenylate: the mechanism of discrimination between asparagine and aspartic acid.
  EMBO J, 17, 2947-2960.  
10089514 C.Briand, A.Poterszman, A.Mitschler, M.Yusupov, J.C.Thierry, and D.Moras (1998).
Crystals of Thermus thermophilus tRNAAsp complexed with its cognate aspartyl-tRNA synthetase have a solvent content of 75%. Comparison with other aminoacylation systems.
  Acta Crystallogr D Biol Crystallogr, 54, 1382-1386.  
9814764 C.S.Vörtler, O.Fedorova, T.Persson, U.Kutzke, and F.Eckstein (1998).
Determination of 2'-hydroxyl and phosphate groups important for aminoacylation of Escherichia coli tRNAAsp: a nucleotide analogue interference study.
  RNA, 4, 1444-1454.  
9622512 C.Stehlin, B.Burke, F.Yang, H.Liu, K.Shiba, and K.Musier-Forsyth (1998).
Species-specific differences in the operational RNA code for aminoacylation of tRNAPro.
  Biochemistry, 37, 8605-8613.  
9587002 D.M.Briercheck, T.C.Wood, T.J.Allison, J.P.Richardson, and G.S.Rule (1998).
The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions.
  Nat Struct Biol, 5, 393-399.
PDB code: 1a63
9724658 E.Schmitt, L.Moulinier, S.Fujiwara, T.Imanaka, J.C.Thierry, and D.Moras (1998).
Crystal structure of aspartyl-tRNA synthetase from Pyrococcus kodakaraensis KOD: archaeon specificity and catalytic mechanism of adenylate formation.
  EMBO J, 17, 5227-5237.
PDB codes: 1b8a 3nel 3nem 3nen
9605503 I.Landrieu, M.Vandenbol, R.Leberman, D.Portetelle, and M.Hartlein (1998).
Identification of YHR019 in Saccharomyces cerevisiae chromosome VIII as the gene for the cytosolic asparaginyl-tRNA synthetase.
  Yeast, 14, 527-533.  
9736621 J.Cavarelli, B.Delagoutte, G.Eriani, J.Gangloff, and D.Moras (1998).
L-arginine recognition by yeast arginyl-tRNA synthetase.
  EMBO J, 17, 5438-5448.
PDB code: 1bs2
9493270 J.L.Kim, K.A.Morgenstern, J.P.Griffith, M.D.Dwyer, J.A.Thomson, M.A.Murcko, C.Lin, and P.R.Caron (1998).
Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding.
  Structure, 6, 89.
PDB code: 1a1v
9857205 J.M.Ryter, and S.C.Schultz (1998).
Molecular basis of double-stranded RNA-protein interactions: structure of a dsRNA-binding domain complexed with dsRNA.
  EMBO J, 17, 7505-7513.
PDB code: 1di2
9636067 J.W.Chihade, K.Hayashibara, K.Shiba, and P.Schimmel (1998).
Strong selective pressure to use G:U to mark an RNA acceptor stem for alanine.
  Biochemistry, 37, 9193-9202.  
9736622 L.Ribas de Pouplana, D.Buechter, N.Y.Sardesai, and P.Schimmel (1998).
Functional analysis of peptide motif for RNA microhelix binding suggests new family of RNA-binding domains.
  EMBO J, 17, 5449-5457.  
9722650 M.Gerstein, and W.Krebs (1998).
A database of macromolecular motions.
  Nucleic Acids Res, 26, 4280-4290.  
9875850 M.P.Horvath, V.L.Schweiker, J.M.Bevilacqua, J.A.Ruggles, and S.C.Schultz (1998).
Crystal structure of the Oxytricha nova telomere end binding protein complexed with single strand DNA.
  Cell, 95, 963-974.
PDB code: 1otc
10333745 R.N.De Guzman, R.B.Turner, and M.F.Summers (1998).
Protein-RNA recognition.
  Biopolymers, 48, 181-195.  
9770466 R.W.Alexander, B.E.Nordin, and P.Schimmel (1998).
Activation of microhelix charging by localized helix destabilization.
  Proc Natl Acad Sci U S A, 95, 12214-12219.  
9585560 T.M.Thompson, B.L.Mark, C.W.Gray, T.C.Terwilliger, N.Sreerama, R.W.Woody, and D.M.Gray (1998).
Circular dichroism and electron microscopy of a core Y61F mutant of the F1 gene 5 single-stranded DNA-binding protein and theoretical analysis of CD spectra of four Tyr --> Phe substitutions.
  Biochemistry, 37, 7463-7477.  
9437423 T.Nakatsu, H.Kato, and J.Oda (1998).
Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase.
  Nat Struct Biol, 5, 15-19.
PDB codes: 11as 12as
9562563 V.L.Rath, L.F.Silvian, B.Beijer, B.S.Sproat, and T.A.Steitz (1998).
How glutaminyl-tRNA synthetase selects glutamine.
  Structure, 6, 439-449.
PDB code: 1qtq
9843398 V.Ramesh, S.Gite, and U.L.RajBhandary (1998).
Functional interaction of an arginine conserved in the sixteen amino acid insertion module of Escherichia coli methionyl-tRNA formyltransferase with determinants for formylation in the initiator tRNA.
  Biochemistry, 37, 15925-15932.  
9435214 W.H.McClain, J.Schneider, S.Bhattacharya, and K.Gabriel (1998).
The importance of tRNA backbone-mediated interactions with synthetase for aminoacylation.
  Proc Natl Acad Sci U S A, 95, 460-465.  
9115984 A.Aberg, A.Yaremchuk, M.Tukalo, B.Rasmussen, and S.Cusack (1997).
Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase.
  Biochemistry, 36, 3084-3094.
PDB codes: 1adj 1ady
9153306 A.Ramos, and G.Varani (1997).
Structure of the acceptor stem of Escherichia coli tRNA Ala: role of the G3.U70 base pair in synthetase recognition.
  Nucleic Acids Res, 25, 2083-2090.
PDB code: 1ikd
9358165 A.U.Metzger, M.Heckl, D.Willbold, K.Breitschopf, U.L.RajBhandary, P.Rösch, and H.J.Gross (1997).
Structural studies on tRNA acceptor stem microhelices: exchange of the discriminator base A73 for G in human tRNALeu switches the acceptor specificity from leucine to serine possibly by decreasing the stability of the terminal G1-C72 base pair.
  Nucleic Acids Res, 25, 4551-4556.  
9032056 B.F.Clark, and J.Nyborg (1997).
The ternary complex of EF-Tu and its role in protein biosynthesis.
  Curr Opin Struct Biol, 7, 110-116.  
9185564 B.Lustig, S.Arora, and R.L.Jernigan (1997).
RNA base-amino acid interaction strengths derived from structures and sequences.
  Nucleic Acids Res, 25, 2562-2565.  
9222494 C.S.Hamann, and Y.M.Hou (1997).
A strategy of tRNA recognition that includes determinants of RNA structure.
  Bioorg Med Chem, 5, 1011-1019.  
9062123 C.Stehlin, D.H.Heacock, H.Liu, and K.Musier-Forsyth (1997).
Chemical modification and site-directed mutagenesis of the single cysteine in motif 3 of class II Escherichia coli prolyl-tRNA synthetase.
  Biochemistry, 36, 2932-2938.  
9294168 D.R.Liu, T.J.Magliery, M.Pastrnak, and P.G.Schultz (1997).
Engineering a tRNA and aminoacyl-tRNA synthetase for the site-specific incorporation of unnatural amino acids into proteins in vivo.
  Proc Natl Acad Sci U S A, 94, 10092-10097.  
  9171418 F.Martin, G.J.Sharples, R.G.Lloyd, S.Eiler, D.Moras, J.Gangloff, and G.Eriani (1997).
Characterization of a thermosensitive Escherichia coli aspartyl-tRNA synthetase mutant.
  J Bacteriol, 179, 3691-3696.  
  9194182 G.S.Prasad, R.Radhakrishnan, D.T.Mitchell, C.A.Earhart, M.M.Dinges, W.J.Cook, P.M.Schlievert, and D.H.Ohlendorf (1997).
Refined structures of three crystal forms of toxic shock syndrome toxin-1 and of a tetramutant with reduced activity.
  Protein Sci, 6, 1220-1227.
PDB codes: 2tss 3tss 4tss 5tss
9222493 J.Rudinger, B.Felden, C.Florentz, and R.Giegé (1997).
Strategy for RNA recognition by yeast histidyl-tRNA synthetase.
  Bioorg Med Chem, 5, 1001-1009.  
9433122 K.Shiba, H.Motegi, and P.Schimmel (1997).
Maintaining genetic code through adaptations of tRNA synthetases to taxonomic domains.
  Trends Biochem Sci, 22, 453-457.  
9135158 M.Sette, P.van Tilborg, R.Spurio, R.Kaptein, M.Paci, C.O.Gualerzi, and R.Boelens (1997).
The structure of the translational initiation factor IF1 from E.coli contains an oligomer-binding motif.
  EMBO J, 16, 1436-1443.
PDB code: 1ah9
9396794 M.Sissler, G.Eriani, F.Martin, R.Giegé, and C.Florentz (1997).
Mirror image alternative interaction patterns of the same tRNA with either class I arginyl-tRNA synthetase or class II aspartyl-tRNA synthetase.
  Nucleic Acids Res, 25, 4899-4906.  
9405377 S.E.Butcher, T.Dieckmann, and J.Feigon (1997).
Solution structure of a GAAA tetraloop receptor RNA.
  EMBO J, 16, 7490-7499.
PDB code: 1tlr
9097731 S.R.Holbrook, and S.H.Kim (1997).
RNA crystallography.
  Biopolymers, 44, 3.  
9192620 S.Raghunathan, C.S.Ricard, T.M.Lohman, and G.Waksman (1997).
Crystal structure of the homo-tetrameric DNA binding domain of Escherichia coli single-stranded DNA-binding protein determined by multiwavelength x-ray diffraction on the selenomethionyl protein at 2.9-A resolution.
  Proc Natl Acad Sci U S A, 94, 6652-6657.
PDB code: 1kaw
9016717 Y.Goldgur, L.Mosyak, L.Reshetnikova, V.Ankilova, O.Lavrik, S.Khodyreva, and M.Safro (1997).
The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe.
  Structure, 5, 59-68.
PDB code: 1eiy
9190291 Y.M.Hou (1997).
Discriminating among the discriminator bases of tRNAs.
  Chem Biol, 4, 93-96.  
8612277 A.E.Hodel, P.D.Gershon, X.Shi, and F.A.Quiocho (1996).
The 1.85 A structure of vaccinia protein VP39: a bifunctional enzyme that participates in the modification of both mRNA ends.
  Cell, 85, 247-256.
PDB code: 1vpt
8805509 C.Davies, S.W.White, and V.Ramakrishnan (1996).
The crystal structure of ribosomal protein L14 reveals an important organizational component of the translational apparatus.
  Structure, 4, 55-66.
PDB code: 1whi
  8654383 C.Romier, K.Reuter, D.Suck, and R.Ficner (1996).
Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange.
  EMBO J, 15, 2850-2857.
PDB code: 1pud
8916927 D.W.Ohannesian, J.Oh, and Y.M.Hou (1996).
Mutational analysis of a leucine heptad repeat motif in a class I aminoacyl-tRNA synthetase.
  Biochemistry, 35, 14405-14412.  
  8887566 E.Schmitt, S.Blanquet, and Y.Mechulam (1996).
Structure of crystalline Escherichia coli methionyl-tRNA(f)Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase.
  EMBO J, 15, 4749-4758.
PDB code: 1fmt
8652522 H.D.Becker, R.Giegé, and D.Kern (1996).
Identity of prokaryotic and eukaryotic tRNA(Asp) for aminoacylation by aspartyl-tRNA synthetase from Thermus thermophilus.
  Biochemistry, 35, 7447-7458.  
8710865 J.A.Enríquez, and G.Attardi (1996).
Evidence for aminoacylation-induced conformational changes in human mitochondrial tRNAs.
  Proc Natl Acad Sci U S A, 93, 8300-8305.  
8942633 J.G.Arnez, and T.A.Steitz (1996).
Crystal structures of three misacylating mutants of Escherichia coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP.
  Biochemistry, 35, 14725-14733.
PDB codes: 1qrs 1qrt 1qru
8652564 J.Tao, and A.D.Frankel (1996).
Arginine-binding RNAs resembling TAR identified by in vitro selection.
  Biochemistry, 35, 2229-2238.  
8602350 K.Breitschopf, and H.J.Gross (1996).
The discriminator bases G73 in human tRNA(Ser) and A73 in tRNA(Leu) have significantly different roles in the recognition of aminoacyl-tRNA synthetases.
  Nucleic Acids Res, 24, 405-410.  
8679560 L.Ribas de Pouplana, D.S.Auld, S.Kim, and P.Schimmel (1996).
A mechanism for reducing entropic cost of induced fit in protein--RNA recognition.
  Biochemistry, 35, 8095-8102.  
  8654382 M.E.Saks, and J.R.Sampson (1996).
Variant minihelix RNAs reveal sequence-specific recognition of the helical tRNA(Ser) acceptor stem by E.coli seryl-tRNA synthetase.
  EMBO J, 15, 2843-2849.  
8944770 M.H.Mazauric, J.Reinbolt, B.Lorber, C.Ebel, G.Keith, R.Giegé, and D.Kern (1996).
An example of non-conservation of oligomeric structure in prokaryotic aminoacyl-tRNA synthetases. Biochemical and structural properties of glycyl-tRNA synthetase from Thermus thermophilus.
  Eur J Biochem, 241, 814-826.  
8842234 P.Auffinger, and E.Westhof (1996).
H-bond stability in the tRNA(Asp) anticodon hairpin: 3 ns of multiple molecular dynamics simulations.
  Biophys J, 71, 940-954.  
8756460 P.C.Bevilacqua, and T.R.Cech (1996).
Minor-groove recognition of double-stranded RNA by the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR.
  Biochemistry, 35, 9983-9994.  
8804834 P.J.Hagerman, and K.M.Amiri (1996).
Hammering away at RNA global structure.
  Curr Opin Struct Biol, 6, 317-321.  
  8918475 P.Romby, J.Caillet, C.Ebel, C.Sacerdot, M.Graffe, F.Eyermann, C.Brunel, H.Moine, C.Ehresmann, B.Ehresmann, and M.Springer (1996).
The expression of E.coli threonyl-tRNA synthetase is regulated at the translational level by symmetrical operator-repressor interactions.
  EMBO J, 15, 5976-5987.  
8555164 R.Aphasizhev, B.Senger, J.U.Rengers, M.Sprinzl, P.Walter, G.Nussbaum, and F.Fasiolo (1996).
Conservation in evolution for a small monomeric phenylalanyl-tRNA synthetase of the tRNA(Phe) recognition nucleotides and initial aminoacylation site.
  Biochemistry, 35, 117-123.  
  8654381 S.Cusack, A.Yaremchuk, and M.Tukalo (1996).
The crystal structure of the ternary complex of T.thermophilus seryl-tRNA synthetase with tRNA(Ser) and a seryl-adenylate analogue reveals a conformational switch in the active site.
  EMBO J, 15, 2834-2842.  
  8947055 S.Cusack, A.Yaremchuk, and M.Tukalo (1996).
The crystal structures of T. thermophilus lysyl-tRNA synthetase complexed with E. coli tRNA(Lys) and a T. thermophilus tRNA(Lys) transcript: anticodon recognition and conformational changes upon binding of a lysyl-adenylate analogue.
  EMBO J, 15, 6321-6334.  
8610114 S.P.Hale, and P.Schimmel (1996).
Protein synthesis editing by a DNA aptamer.
  Proc Natl Acad Sci U S A, 93, 2755-2758.  
8643439 S.Rodin, A.Rodin, and S.Ohno (1996).
The presence of codon-anticodon pairs in the acceptor stem of tRNAs.
  Proc Natl Acad Sci U S A, 93, 4537-4542.  
8810901 T.Hara, H.Kato, Y.Katsube, and J.Oda (1996).
A pseudo-michaelis quaternary complex in the reverse reaction of a ligase: structure of Escherichia coli B glutathione synthetase complexed with ADP, glutathione, and sulfate at 2.0 A resolution.
  Biochemistry, 35, 11967-11974.
PDB code: 1gsa
  8601277 W.H.McClain, K.Gabriel, and J.Schneider (1996).
Specific function of a G.U wobble pair from an adjacent helical site in tRNA(Ala) during recognition by alanyl-tRNA synthetase.
  RNA, 2, 105-109.  
8639604 W.Yan, J.Augustine, and C.Francklyn (1996).
A tRNA identity switch mediated by the binding interaction between a tRNA anticodon and the accessory domain of a class II aminoacyl-tRNA synthetase.
  Biochemistry, 35, 6559-6568.  
7540304 A.D.Yaremchuk, I.A.Krikliviy, S.Cusack, and M.A.Tukalo (1995).
Cocrystallization of lysyl-tRNA synthetase from Thermus thermophilus with its cognate tRNAlys and with Escherichia coli tRNAlys.
  Proteins, 21, 261-264.  
7479716 A.D.Yaremchuk, S.Cusack, A.Aberg, O.Gudzera, I.Kryklivyi, and M.Tukalo (1995).
Crystallization of Thermus thermophilus histidyl-tRNA synthetase and its complex with tRNAHis.
  Proteins, 22, 426-428.  
7537870 C.Vincent, F.Borel, J.C.Willison, R.Leberman, and M.Härtlein (1995).
Seryl-tRNA synthetase from Escherichia coli: functional evidence for cross-dimer tRNA binding during aminoacylation.
  Nucleic Acids Res, 23, 1113-1118.  
7540101 D.Moras, and A.Poterszman (1995).
RNA-protein interactions. Diverse modes of recognition.
  Curr Biol, 5, 249-251.  
  7556056 D.T.Logan, M.H.Mazauric, D.Kern, and D.Moras (1995).
Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus.
  EMBO J, 14, 4156-4167.
PDB code: 1ati
8532520 E.Schmitt, M.Panvert, S.Blanquet, and Y.Mechulam (1995).
Transition state stabilization by the 'high' motif of class I aminoacyl-tRNA synthetases: the case of Escherichia coli methionyl-tRNA synthetase.
  Nucleic Acids Res, 23, 4793-4798.  
7613865 H.Belrhali, A.Yaremchuk, M.Tukalo, C.Berthet-Colominas, B.Rasmussen, P.Bösecke, O.Diat, and S.Cusack (1995).
The structural basis for seryl-adenylate and Ap4A synthesis by seryl-tRNA synthetase.
  Structure, 3, 341-352.  
7870582 H.Liu, R.Peterson, J.Kessler, and K.Musier-Forsyth (1995).
Molecular recognition of tRNA(Pro) by Escherichia coli proline tRNA synthetase in vitro.
  Nucleic Acids Res, 23, 165-169.  
  7556055 J.G.Arnez, D.C.Harris, A.Mitschler, B.Rees, C.S.Francklyn, and D.Moras (1995).
Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate.
  EMBO J, 14, 4143-4155.
PDB code: 1htt
  8846773 K.Harada, and A.D.Frankel (1995).
Identification of two novel arginine binding DNAs.
  EMBO J, 14, 5798-5811.  
7761451 L.Chen, and A.D.Frankel (1995).
A peptide interaction in the major groove of RNA resembles protein interactions in the minor groove of DNA.
  Proc Natl Acad Sci U S A, 92, 5077-5081.  
7664121 L.Mosyak, L.Reshetnikova, Y.Goldgur, M.Delarue, and M.G.Safro (1995).
Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus.
  Nat Struct Biol, 2, 537-547.
PDB code: 1pys
7773747 M.Delarue (1995).
Aminoacyl-tRNA synthetases.
  Curr Opin Struct Biol, 5, 48-55.  
  8563641 M.Safro, and L.Mosyak (1995).
Structural similarities in the noncatalytic domains of phenylalanyl-tRNA and biotin synthetases.
  Protein Sci, 4, 2429-2432.  
7761403 M.W.Friederich, F.U.Gast, E.Vacano, and P.J.Hagerman (1995).
Determination of the angle between the anticodon and aminoacyl acceptor stems of yeast phenylalanyl tRNA in solution.
  Proc Natl Acad Sci U S A, 92, 4803-4807.  
7885835 N.Nameki, H.Asahara, M.Shimizu, N.Okada, and H.Himeno (1995).
Identity elements of Saccharomyces cerevisiae tRNA(His).
  Nucleic Acids Res, 23, 389-394.  
7878729 P.Schimmel, and E.Schmidt (1995).
Making connections: RNA-dependent amino acid recognition.
  Trends Biochem Sci, 20, 1-2.  
8524648 R.Kreutzer, D.Kern, R.Giegé, and J.Rudinger (1995).
Footprinting of tRNA(Phe) transcripts from Thermus thermophilus HB8 with the homologous phenylalanyl-tRNA synthetase reveals a novel mode of interaction.
  Nucleic Acids Res, 23, 4598-4602.  
7777498 R.Tan, and A.D.Frankel (1995).
Structural variety of arginine-rich RNA-binding peptides.
  Proc Natl Acad Sci U S A, 92, 5282-5286.  
  7623840 S.A.Wek, S.Zhu, and R.C.Wek (1995).
The histidyl-tRNA synthetase-related sequence in the eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids.
  Mol Cell Biol, 15, 4497-4506.  
7552701 S.Cusack (1995).
Eleven down and nine to go.
  Nat Struct Biol, 2, 824-831.  
7494636 S.N.Rodin, and S.Ohno (1995).
Two types of aminoacyl-tRNA synthetases could be originally encoded by complementary strands of the same nucleic acid.
  Orig Life Evol Biosph, 25, 565-589.  
7735833 S.Onesti, A.D.Miller, and P.Brick (1995).
The crystal structure of the lysyl-tRNA synthetase (LysU) from Escherichia coli.
  Structure, 3, 163-176.
PDB code: 1lyl
7761427 T.L.Ripmaster, K.Shiba, and P.Schimmel (1995).
Wide cross-species aminoacyl-tRNA synthetase replacement in vivo: yeast cytoplasmic alanine enzyme replaced by human polymyositis serum antigen.
  Proc Natl Acad Sci U S A, 92, 4932-4936.  
  7576245 W.Freist, and D.H.Gauss (1995).
Lysyl-tRNA synthetase.
  Biol Chem Hoppe Seyler, 376, 451-472.  
  7969132 C.R.Vazquez de Aldana, R.C.Wek, P.S.Segundo, A.G.Truesdell, and A.G.Hinnebusch (1994).
Multicopy tRNA genes functionally suppress mutations in yeast eIF-2 alpha kinase GCN2: evidence for separate pathways coupling GCN4 expression to unchanged tRNA.
  Mol Cell Biol, 14, 7920-7932.  
7937159 D.R.Wolstenholme, R.Okimoto, and J.L.Macfarlane (1994).
Nucleotide correlations that suggest tertiary interactions in the TV-replacement loop-containing mitochondrial tRNAs of the nematodes, Caenorhabditis elegans and Ascaris suum.
  Nucleic Acids Res, 22, 4300-4306.  
8065908 F.Borel, C.Vincent, R.Leberman, and M.Härtlein (1994).
Seryl-tRNA synthetase from Escherichia coli: implication of its N-terminal domain in aminoacylation activity and specificity.
  Nucleic Acids Res, 22, 2963-2969.  
  8139004 F.Houser-Scott, M.L.Baer, K.F.Liem, J.M.Cai, and L.Gehrke (1994).
Nucleotide sequence and structural determinants of specific binding of coat protein or coat protein peptides to the 3' untranslated region of alfalfa mosaic virus RNA 4.
  J Virol, 68, 2194-2205.  
  8313877 J.Cavarelli, G.Eriani, B.Rees, M.Ruff, M.Boeglin, A.Mitschler, F.Martin, J.Gangloff, J.C.Thierry, and D.Moras (1994).
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction.
  EMBO J, 13, 327-337.
PDB code: 1asz
  8169220 J.Chen, A.Brevet, M.Lapadat-Tapolsky, S.Blanquet, and P.Plateau (1994).
Properties of the lysyl-tRNA synthetase gene and product from the extreme thermophile Thermus thermophilus.
  J Bacteriol, 176, 2699-2705.  
7800496 J.Rudinger, C.Florentz, and R.Giegé (1994).
Histidylation by yeast HisRS of tRNA or tRNA-like structure relies on residues -1 and 73 but is dependent on the RNA context.
  Nucleic Acids Res, 22, 5031-5037.  
7830558 L.Bénard, C.Philippe, L.Dondon, M.Grunberg-Manago, B.Ehresmann, C.Ehresmann, and C.Portier (1994).
Mutational analysis of the pseudoknot structure of the S15 translational operator from Escherichia coli.
  Mol Microbiol, 14, 31-40.  
  8045252 M.Delarue, A.Poterszman, S.Nikonov, M.Garber, D.Moras, and J.C.Thierry (1994).
Crystal structure of a prokaryotic aspartyl tRNA-synthetase.
  EMBO J, 13, 3219-3229.  
  8313916 M.L.Baer, F.Houser, L.S.Loesch-Fries, and L.Gehrke (1994).
Specific RNA binding by amino-terminal peptides of alfalfa mosaic virus coat protein.
  EMBO J, 13, 727-735.  
8041690 N.Maizels, and A.M.Weiner (1994).
Phylogeny from function: evidence from the molecular fossil record that tRNA originated in replication, not translation.
  Proc Natl Acad Sci U S A, 91, 6729-6734.  
7634083 P.J.Artymiuk, D.W.Rice, A.R.Poirrette, and P.Willet (1994).
A tale of two synthetases.
  Nat Struct Biol, 1, 758-760.  
7972050 P.Schimmel, and B.Henderson (1994).
Possible role of aminoacyl-RNA complexes in noncoded peptide synthesis and origin of coded synthesis.
  Proc Natl Acad Sci U S A, 91, 11283-11286.  
8127693 W.H.McClain, J.Schneider, and K.Gabriel (1994).
Distinctive acceptor-end structure and other determinants of Escherichia coli tRNAPro identity.
  Nucleic Acids Res, 22, 522-529.  
  8458342 A.G.Murzin (1993).
OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences.
  EMBO J, 12, 861-867.  
8441673 C.A.Menguito, M.J.Keherly, C.Tang, J.Papaconstantinou, and P.H.Weigel (1993).
Molecular cloning, sequence, structural analysis and expression of the histidyl-tRNA synthetase gene from Streptococcus equisimilis.
  Nucleic Acids Res, 21, 615-620.  
8346229 C.P.Lee, N.Mandal, M.R.Dyson, and U.L.RajBhandary (1993).
The discriminator base influences tRNA structure at the end of the acceptor stem and possibly its interaction with proteins.
  Proc Natl Acad Sci U S A, 90, 7149-7152.  
  7691478 D.D.Buechter, and P.Schimmel (1993).
Aminoacylation of RNA minihelices: implications for tRNA synthetase structural design and evolution.
  Crit Rev Biochem Mol Biol, 28, 309-322.  
  7505222 E.Schwob, and D.Söll (1993).
Selection of a 'minimal' glutaminyl-tRNA synthetase and the evolution of class I synthetases.
  EMBO J, 12, 5201-5208.  
8248175 G.Eriani, J.Cavarelli, F.Martin, G.Dirheimer, D.Moras, and J.Gangloff (1993).
Role of dimerization in yeast aspartyl-tRNA synthetase and importance of the class II invariant proline.
  Proc Natl Acad Sci U S A, 90, 10816-10820.  
7680483 I.Weygand-Durasević, E.Schwob, and D.Söll (1993).
Acceptor end binding domain interactions ensure correct aminoacylation of transfer RNA.
  Proc Natl Acad Sci U S A, 90, 2010-2014.  
8460131 J.A.Landro, and P.Schimmel (1993).
Metal-binding site in a class I tRNA synthetase localized to a cysteine cluster inserted into nucleotide-binding fold.
  Proc Natl Acad Sci U S A, 90, 2261-2265.  
8441619 J.D.Puglisi, J.Pütz, C.Florentz, and R.Giegé (1993).
Influence of tRNA tertiary structure and stability on aminoacylation by yeast aspartyl-tRNA synthetase.
  Nucleic Acids Res, 21, 41-49.  
7682716 J.D.Puglisi, L.Chen, A.D.Frankel, and J.R.Williamson (1993).
Role of RNA structure in arginine recognition of TAR RNA.
  Proc Natl Acad Sci U S A, 90, 3680-3684.  
  8335008 J.Pütz, J.D.Puglisi, C.Florentz, and R.Giegé (1993).
Additive, cooperative and anti-cooperative effects between identity nucleotides of a tRNA.
  EMBO J, 12, 2949-2957.  
7694078 K.Nagai (1993).
Recent advances in RNA-protein interaction studies.
  Mol Biol Rep, 18, 105-112.  
  8298469 L.Ribas de Pouplana, D.D.Buechter, M.W.Davis, and P.Schimmel (1993).
Idiographic representation of conserved domain of a class II tRNA synthetase of unknown structure.
  Protein Sci, 2, 2259-2262.  
8274143 M.Delarue, and D.Moras (1993).
The aminoacyl-tRNA synthetase family: modules at work.
  Bioessays, 15, 675-687.  
7692438 P.Schimmel, R.Giegé, D.Moras, and S.Yokoyama (1993).
An operational RNA code for amino acids and possible relationship to genetic code.
  Proc Natl Acad Sci U S A, 90, 8763-8768.  
7684657 R.Tan, L.Chen, J.A.Buettner, D.Hudson, and A.D.Frankel (1993).
RNA recognition by an isolated alpha helix.
  Cell, 73, 1031-1040.  
8341698 Y.M.Hou, E.Westhof, and R.Giegé (1993).
An unusual RNA tertiary interaction has a role for the specific aminoacylation of a transfer RNA.
  Proc Natl Acad Sci U S A, 90, 6776-6780.  
8256282 Y.M.Hou (1993).
The tertiary structure of tRNA and the development of the genetic code.
  Trends Biochem Sci, 18, 362-364.  
  1304886 A.D.Frankel (1992).
Peptide models of the Tat-TAR protein-RNA interaction.
  Protein Sci, 1, 1539-1542.  
1375910 C.Francklyn, K.Musier-Forsyth, and P.Schimmel (1992).
Small RNA helices as substrates for aminoacylation and their relationship to charging of transfer RNAs.
  Eur J Biochem, 206, 315-321.  
1544480 D.Madern, J.Anselme, and M.Härtlein (1992).
Asparaginyl-tRNA synthetase from the Escherichia coli temperature-sensitive strain HO202. A proline replacement in motif 2 is responsible for a large increase in Km for asparagine and ATP.
  FEBS Lett, 299, 85-89.  
1585461 D.Moras (1992).
Structural and functional relationships between aminoacyl-tRNA synthetases.
  Trends Biochem Sci, 17, 159-164.  
1425658 H.Aoki, P.J.Yaworsky, S.D.Patel, D.Margolin-Brzezinski, K.S.Park, and M.C.Ganoza (1992).
The asparaginyl-tRNA synthetase gene encodes one of the complementing factors for thermosensitive translation in the Escherichia coli mutant strain, N4316.
  Eur J Biochem, 209, 511-521.  
  1735715 I.Wower, M.P.Kowaleski, L.E.Sears, and R.A.Zimmermann (1992).
Mutagenesis of ribosomal protein S8 from Escherichia coli: defects in regulation of the spc operon.
  J Bacteriol, 174, 1213-1221.  
1454353 J.C.Lacey, N.S.Wickramasinghe, G.W.Cook, and J.C.Lacey (1992).
Experimental studies on the origin of the genetic code and the process of protein synthesis: a review update.
  Orig Life Evol Biosph, 22, 243-275.  
  1304356 J.J.Burbaum, and P.Schimmel (1992).
Amino acid binding by the class I aminoacyl-tRNA synthetases: role for a conserved proline in the signature sequence.
  Protein Sci, 1, 575-581.  
1377381 J.M.Sherman, M.J.Rogers, and D.Söll (1992).
Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation.
  Nucleic Acids Res, 20, 2847-2852.  
16617497 J.M.Sherman, M.J.Rogers, and D.Söll (1992).
Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation.
  Nucleic Acids Res, 20, 1547-1552.  
1631068 J.Rudinger, J.D.Puglisi, J.Pütz, D.Schatz, F.Eckstein, C.Florentz, and R.Giegé (1992).
Determinant nucleotides of yeast tRNA(Asp) interact directly with aspartyl-tRNA synthetase.
  Proc Natl Acad Sci U S A, 89, 5882-5886.  
1557378 J.Tao, and A.D.Frankel (1992).
Specific binding of arginine to TAR RNA.
  Proc Natl Acad Sci U S A, 89, 2723-2726.  
1521534 L.Reshetnikova, M.Chernaya, V.Ankilova, O.Lavrik, M.Delarue, J.C.Thierry, D.Moras, and M.Safro (1992).
Three-dimensional structure of phenylalanyl-transfer RNA synthetase from Thermus thermophilus HB8 at 0.6-nm resolution.
  Eur J Biochem, 208, 411-417.  
  1448107 M.Ramirez, R.C.Wek, C.R.Vazquez de Aldana, B.M.Jackson, B.Freeman, and A.G.Hinnebusch (1992).
Mutations activating the yeast eIF-2 alpha kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases.
  Mol Cell Biol, 12, 5801-5815.  
1549469 N.Raben, F.Borriello, J.Amin, R.Horwitz, D.Fraser, and P.Plotz (1992).
Human histidyl-tRNA synthetase: recognition of amino acid signature regions in class 2a aminoacyl-tRNA synthetases.
  Nucleic Acids Res, 20, 1075-1081.  
1280807 P.Romby, C.Brunel, J.Caillet, M.Springer, M.Grunberg-Manago, E.Westhof, C.Ehresmann, and B.Ehresmann (1992).
Molecular mimicry in translational control of E. coli threonyl-tRNA synthetase gene. Competitive inhibition in tRNA aminoacylation and operator-repressor recognition switch using tRNA identity rules.
  Nucleic Acids Res, 20, 5633-5640.  
1508711 R.Kreutzer, V.Kruft, E.V.Bobkova, O.I.Lavrik, and M.Sprinzl (1992).
Structure of the phenylalanyl-tRNA synthetase genes from Thermus thermophilus HB8 and their expression in Escherichia coli.
  Nucleic Acids Res, 20, 4173-4178.  
1628641 R.Martinez, and M.Mirande (1992).
The polyanion-binding domain of cytoplasmic Lys-tRNA synthetase from Saccharomyces cerevisiae is not essential for cell viability.
  Eur J Biochem, 207, 1.  
1729719 S.A.Martinis, and P.Schimmel (1992).
Enzymatic aminoacylation of sequence-specific RNA minihelices and hybrid duplexes with methionine.
  Proc Natl Acad Sci U S A, 89, 65-69.  
1579445 S.Beresten, M.Jahn, and D.Söll (1992).
Aminoacyl-tRNA synthetase-induced cleavage of tRNA.
  Nucleic Acids Res, 20, 1523-1530.  
  1560535 U.Delling, L.S.Reid, R.W.Barnett, M.Y.Ma, S.Climie, M.Sumner-Smith, and N.Sonenberg (1992).
Conserved nucleotides in the TAR RNA stem of human immunodeficiency virus type 1 are critical for Tat binding and trans activation: model for TAR RNA tertiary structure.
  J Virol, 66, 3018-3025.  
1614849 V.Lim, C.Venclovas, A.Spirin, R.Brimacombe, P.Mitchell, and F.Müller (1992).
How are tRNAs and mRNA arranged in the ribosome? An attempt to correlate the stereochemistry of the tRNA-mRNA interaction with constraints imposed by the ribosomal topography.
  Nucleic Acids Res, 20, 2627-2637.  
  1396597 Y.Hayase, M.Jahn, M.J.Rogers, L.A.Sylvers, M.Koizumi, H.Inoue, E.Ohtsuka, and D.Söll (1992).
Recognition of bases in Escherichia coli tRNA(Gln) by glutaminyl-tRNA synthetase: a complete identity set.
  EMBO J, 11, 4159-4165.  
  1756734 C.Cerini, P.Kerjan, M.Astier, D.Gratecos, M.Mirande, and M.Sémériva (1991).
A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase.
  EMBO J, 10, 4267-4277.  
1763051 C.P.Lee, and U.L.RajBhandary (1991).
Mutants of Escherichia coli initiator tRNA that suppress amber codons in Saccharomyces cerevisiae and are aminoacylated with tyrosine by yeast extracts.
  Proc Natl Acad Sci U S A, 88, 11378-11382.  
1721699 H.Himeno, T.Hasegawa, H.Asahara, K.Tamura, and M.Shimizu (1991).
Identity determinants of E. coli tryptophan tRNA.
  Nucleic Acids Res, 19, 6379-6382.  
1924390 W.H.McClain, K.Foss, R.A.Jenkins, and J.Schneider (1991).
Four sites in the acceptor helix and one site in the variable pocket of tRNA(Ala) determine the molecule's acceptor identity.
  Proc Natl Acad Sci U S A, 88, 9272-9276.  
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