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PDBsum entry 1eft

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protein ligands metals links
Elongation factor PDB id
1eft
Jmol
Contents
Protein chain
405 a.a. *
Ligands
GNP
Metals
_MG
Waters ×126
* Residue conservation analysis
PDB id:
1eft
Name: Elongation factor
Title: The crystal structure of elongation factor ef-tu from thermu aquaticus in the gtp conformation
Structure: Elongation factor tu. Chain: a. Engineered: yes
Source: Thermus aquaticus. Organism_taxid: 271
Resolution:
2.50Å     R-factor:   0.200    
Authors: M.Kjeldgaard,P.Nissen,S.Thirup,J.Nyborg
Key ref:
M.Kjeldgaard et al. (1993). The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure, 1, 35-50. PubMed id: 8069622
Date:
24-Aug-93     Release date:   31-Aug-94    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q01698  (EFTU_THEAQ) -  Elongation factor Tu
Seq:
Struc:
406 a.a.
405 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     intracellular   2 terms 
  Biological process     translation   3 terms 
  Biochemical function     nucleotide binding     4 terms  

 

 
Structure 1:35-50 (1993)
PubMed id: 8069622  
 
 
The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation.
M.Kjeldgaard, P.Nissen, S.Thirup, J.Nyborg.
 
  ABSTRACT  
 
BACKGROUND: Elongation factor Tu (EF-Tu) is a GTP-binding protein that is crucial for protein biosynthesis. In the GTP form of the molecule, EF-Tu binds tightly to aminoacyl-tRNA, forming a ternary complex that interacts with the ribosomal acceptor site. During this interaction, GTP is hydrolyzed, and EF-Tu.GDP is ejected. RESULTS: The crystal structure of EF-Tu from Thermus aquaticus, complexed to the GTP analogue GDPNP, has been determined at 2.5 A resolution and compared to the structure of Escherichia coli EF-Tu.GDP. During the transition from the GDP (inactive) to the GTP (active) form, domain 1, containing the GTP-binding site, undergoes internal conformational changes similar to those observed in ras-p21. In addition, a dramatic rearrangement of domains is observed, corresponding to a rotation of 90.8 degrees of domain 1 relative to domains 2 and 3. Residues that are affected in the binding of aminoacyl-tRNA are found in or near the cleft formed by the domain interface. CONCLUSION: GTP binding by EF-Tu leads to dramatic conformational changes which expose the tRNA binding site. It appears that tRNA binding to EF-Tu induces a further conformational change, which may affect the GTPase activity.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21152913 K.Kulczycka, M.Długosz, and J.Trylska (2011).
Molecular dynamics of ribosomal elongation factors G and Tu.
  Eur Biophys J, 40, 289-303.  
21151095 M.Y.Pavlov, A.Zorzet, D.I.Andersson, and M.Ehrenberg (2011).
Activation of initiation factor 2 by ligands and mutations for rapid docking of ribosomal subunits.
  EMBO J, 30, 289-301.  
20798060 D.Takeshita, and K.Tomita (2010).
Assembly of Q{beta} viral RNA polymerase with host translational elongation factors EF-Tu and -Ts.
  Proc Natl Acad Sci U S A, 107, 15733-15738.
PDB codes: 3agp 3agq
20876129 K.Kobayashi, I.Kikuno, K.Kuroha, K.Saito, K.Ito, R.Ishitani, T.Inada, and O.Nureki (2010).
Structural basis for mRNA surveillance by archaeal Pelota and GTP-bound EF1α complex.
  Proc Natl Acad Sci U S A, 107, 17575-17579.
PDB code: 3agj
20718859 Y.Chen, R.K.Koripella, S.Sanyal, and M.Selmer (2010).
Staphylococcus aureus elongation factor G--structure and analysis of a target for fusidic acid.
  FEBS J, 277, 3789-3803.
PDB code: 2xex
19416977 A.S.Spirin (2009).
The ribosome as a conveying thermal ratchet machine.
  J Biol Chem, 284, 21103-21119.  
19029250 B.S.Shin, J.R.Kim, M.G.Acker, K.N.Maher, J.R.Lorsch, and T.E.Dever (2009).
rRNA suppressor of a eukaryotic translation initiation factor 5B/initiation factor 2 mutant reveals a binding site for translational GTPases on the small ribosomal subunit.
  Mol Cell Biol, 29, 808-821.  
19122150 E.Villa, J.Sengupta, L.G.Trabuco, J.LeBarron, W.T.Baxter, T.R.Shaikh, R.A.Grassucci, P.Nissen, M.Ehrenberg, K.Schulten, and J.Frank (2009).
Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis.
  Proc Natl Acad Sci U S A, 106, 1063-1068.
PDB codes: 3fih 3fik
19671172 M.Kesimer, N.Kiliç, R.Mehrotra, D.J.Thornton, and J.K.Sheehan (2009).
Identification of salivary mucin MUC7 binding proteins from Streptococcus gordonii.
  BMC Microbiol, 9, 163.  
20025795 X.Agirrezabala, and J.Frank (2009).
Elongation in translation as a dynamic interaction among the ribosome, tRNA, and elongation factors EF-G and EF-Tu.
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18773979 B.L.Grigorenko, M.S.Shadrina, I.A.Topol, J.R.Collins, and A.V.Nemukhin (2008).
Mechanism of the chemical step for the guanosine triphosphate (GTP) hydrolysis catalyzed by elongation factor Tu.
  Biochim Biophys Acta, 1784, 1908-1917.  
18990188 D.L.Hammarlöf, and D.Hughes (2008).
Mutants of the RNA-processing enzyme RNase E reverse the extreme slow-growth phenotype caused by a mutant translation factor EF-Tu.
  Mol Microbiol, 70, 1194-1209.  
18518820 R.A.Marshall, C.E.Aitken, M.Dorywalska, and J.D.Puglisi (2008).
Translation at the single-molecule level.
  Annu Rev Biochem, 77, 177-203.  
18562321 S.B.Ozturk, and T.G.Kinzy (2008).
Guanine nucleotide exchange factor independence of the G-protein eEF1A through novel mutant forms and biochemical properties.
  J Biol Chem, 283, 23244-23253.  
18502805 V.Hauryliuk, S.Hansson, and M.Ehrenberg (2008).
Cofactor dependent conformational switching of GTPases.
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18836081 V.Hauryliuk, V.A.Mitkevich, N.A.Eliseeva, I.Y.Petrushanko, M.Ehrenberg, and A.A.Makarov (2008).
The pretranslocation ribosome is targeted by GTP-bound EF-G in partially activated form.
  Proc Natl Acad Sci U S A, 105, 15678-15683.  
19020518 W.Li, X.Agirrezabala, J.Lei, L.Bouakaz, J.L.Brunelle, R.F.Ortiz-Meoz, R.Green, S.Sanyal, M.Ehrenberg, and J.Frank (2008).
Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM.
  EMBO J, 27, 3322-3331.
PDB codes: 3ep2 3eq3 3eq4
17427948 A.Perdih, M.Kotnik, M.Hodoscek, and T.Solmajer (2007).
Targeted molecular dynamics simulation studies of binding and conformational changes in E. coli MurD.
  Proteins, 68, 243-254.  
17189426 B.S.Shin, M.G.Acker, D.Maag, J.R.Kim, J.R.Lorsch, and T.E.Dever (2007).
Intragenic suppressor mutations restore GTPase and translation functions of a eukaryotic initiation factor 5B switch II mutant.
  Mol Cell Biol, 27, 1677-1685.  
17446867 D.J.Taylor, J.Nilsson, A.R.Merrill, G.R.Andersen, P.Nissen, and J.Frank (2007).
Structures of modified eEF2 80S ribosome complexes reveal the role of GTP hydrolysis in translocation.
  EMBO J, 26, 2421-2431.
PDB codes: 2p8w 2p8x 2p8y 2p8z
17540173 H.Gao, Z.Zhou, U.Rawat, C.Huang, L.Bouakaz, C.Wang, Z.Cheng, Y.Liu, A.Zavialov, R.Gursky, S.Sanyal, M.Ehrenberg, J.Frank, and H.Song (2007).
RF3 induces ribosomal conformational changes responsible for dissociation of class I release factors.
  Cell, 129, 929-941.
PDB codes: 2h5e 2o0f
17328911 L.E.Sanderson, and O.C.Uhlenbeck (2007).
Directed mutagenesis identifies amino acid residues involved in elongation factor Tu binding to yeast Phe-tRNAPhe.
  J Mol Biol, 368, 119-130.  
17337575 L.N.Olsthoorn-Tieleman, R.J.Palstra, G.P.van Wezel, M.J.Bibb, and C.W.Pleij (2007).
Elongation factor Tu3 (EF-Tu3) from the kirromycin producer Streptomyces ramocissimus Is resistant to three classes of EF-Tu-specific inhibitors.
  J Bacteriol, 189, 3581-3590.  
17202208 M.S.Almeida, M.A.Johnson, T.Herrmann, M.Geralt, and K.Wüthrich (2007).
Novel beta-barrel fold in the nuclear magnetic resonance structure of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus.
  J Virol, 81, 3151-3161.
PDB codes: 2gdt 2hsx
17785438 Y.R.Lapik, J.M.Misra, L.F.Lau, and D.G.Pestov (2007).
Restricting conformational flexibility of the switch II region creates a dominant-inhibitory phenotype in Obg GTPase Nog1.
  Mol Cell Biol, 27, 7735-7744.  
16407071 L.Yatime, Y.Mechulam, S.Blanquet, and E.Schmitt (2006).
Structural switch of the gamma subunit in an archaeal aIF2 alpha gamma heterodimer.
  Structure, 14, 119-128.
PDB code: 2aho
16552145 S.E.Heffron, R.Moeller, and F.Jurnak (2006).
Solving the structure of Escherichia coli elongation factor Tu using a twinned data set.
  Acta Crystallogr D Biol Crystallogr, 62, 433-438.
PDB code: 2fx3
15952884 J.M.Ogle, and V.Ramakrishnan (2005).
Structural insights into translational fidelity.
  Annu Rev Biochem, 74, 129-177.  
15557323 M.G.Jeppesen, T.Navratil, L.L.Spremulli, and J.Nyborg (2005).
Crystal structure of the bovine mitochondrial elongation factor Tu.Ts complex.
  J Biol Chem, 280, 5071-5081.
PDB code: 1xb2
15616587 M.Leibundgut, C.Frick, M.Thanbichler, A.Böck, and N.Ban (2005).
Selenocysteine tRNA-specific elongation factor SelB is a structural chimaera of elongation and initiation factors.
  EMBO J, 24, 11-22.
PDB codes: 1wb1 1wb2 1wb3 4ac9 4aca 4acb
15616286 M.M.Jayasekera, K.Onheiber, J.Keith, H.Venkatesan, A.Santillan, E.M.Stocking, L.Tang, J.Miller, L.Gomez, B.Rhead, T.Delcamp, S.Huang, R.Wolin, E.V.Bobkova, and K.J.Shaw (2005).
Identification of novel inhibitors of bacterial translation elongation factors.
  Antimicrob Agents Chemother, 49, 131-136.  
14691225 H.Sanderová, M.Hůlková, P.Malon, M.Kepková, and J.Jonák (2004).
Thermostability of multidomain proteins: elongation factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and their chimeric forms.
  Protein Sci, 13, 89-99.  
14696184 P.J.Focia, H.Alam, T.Lu, U.D.Ramirez, and D.M.Freymann (2004).
Novel protein and Mg2+ configurations in the Mg2+GDP complex of the SRP GTPase ffh.
  Proteins, 54, 222-230.
PDB code: 1o87
12932732 G.R.Andersen, P.Nissen, and J.Nyborg (2003).
Elongation factors in protein biosynthesis.
  Trends Biochem Sci, 28, 434-441.  
14566331 M.Valle, A.Zavialov, W.Li, S.M.Stagg, J.Sengupta, R.C.Nielsen, P.Nissen, S.C.Harvey, M.Ehrenberg, and J.Frank (2003).
Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy.
  Nat Struct Biol, 10, 899-906.
PDB codes: 1qza 1qzb 1qzc 1qzd 1r2w 1r2x
12692531 R.Jørgensen, P.A.Ortiz, A.Carr-Schmid, P.Nissen, T.G.Kinzy, and G.R.Andersen (2003).
Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase.
  Nat Struct Biol, 10, 379-385.
PDB codes: 1n0u 1n0v
12869707 S.Marzi, W.Knight, L.Brandi, E.Caserta, N.Soboleva, W.E.Hill, C.O.Gualerzi, and J.S.Lodmell (2003).
Ribosomal localization of translation initiation factor IF2.
  RNA, 9, 958-969.  
14622005 T.Navratil, and L.L.Spremulli (2003).
Effects of mutagenesis of Gln97 in the switch II region of Escherichia coli elongation factor Tu on its interaction with guanine nucleotides, elongation factor Ts, and aminoacyl-tRNA.
  Biochemistry, 42, 13587-13595.  
12379845 H.Stark, M.V.Rodnina, H.J.Wieden, F.Zemlin, W.Wintermeyer, and M.van Heel (2002).
Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex.
  Nat Struct Biol, 9, 849-854.
PDB code: 1mj1
12403627 J.Petersen, K.Fisher, C.J.Mitchell, and D.J.Lowe (2002).
Multiple inequivalent metal-nucleotide coordination environments in the presence of the VO2+-inhibited nitrogenase iron protein: pH-dependent structural rearrangements at the nucleotide binding site.
  Biochemistry, 41, 13253-13263.  
12093756 M.Valle, J.Sengupta, N.K.Swami, R.A.Grassucci, N.Burkhardt, K.H.Nierhaus, R.K.Agrawal, and J.Frank (2002).
Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process.
  EMBO J, 21, 3557-3567.
PDB codes: 1ls2 1lu3
12145639 T.Ohtsuki, A.Sato, Y.Watanabe, and K.Watanabe (2002).
A unique serine-specific elongation factor Tu found in nematode mitochondria.
  Nat Struct Biol, 9, 669-673.  
12762021 A.D.Wolfson, F.J.LaRiviere, J.A.Pleiss, T.Dale, H.Asahara, and O.C.Uhlenbeck (2001).
tRNA conformity.
  Cold Spring Harb Symp Quant Biol, 66, 185-193.  
12762045 G.R.Andersen, and J.Nyborg (2001).
Structural studies of eukaryotic elongation factors.
  Cold Spring Harb Symp Quant Biol, 66, 425-437.  
11432749 L.N.Olsthoorn-Tieleman, L.J.Plooster, and B.Kraal (2001).
The variant tuf3 gene of Streptomyces coelicolor A3(2) encodes a real elongation factor Tu, as shown in a novel Streptomyces in vitro translation system.
  Eur J Biochem, 268, 3807-3815.  
11574461 L.Vitagliano, M.Masullo, F.Sica, A.Zagari, and V.Bocchini (2001).
The crystal structure of Sulfolobus solfataricus elongation factor 1alpha in complex with GDP reveals novel features in nucleotide binding and exchange.
  EMBO J, 20, 5305-5311.
PDB code: 1jny
11566135 S.Padmanabhan, and D.M.Freymann (2001).
The conformation of bound GMPPNP suggests a mechanism for gating the active site of the SRP GTPase.
  Structure, 9, 859-867.
PDB codes: 1jpj 1jpn
11222280 T.J.Minehardt, R.Cooke, E.Pate, and P.A.Kollman (2001).
Molecular dynamics study of the energetic, mechanistic, and structural implications of a closed phosphate tube in ncd.
  Biophys J, 80, 1151-1168.  
11106763 G.R.Andersen, L.Pedersen, L.Valente, I.Chatterjee, T.G.Kinzy, M.Kjeldgaard, and J.Nyborg (2000).
Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha.
  Mol Cell, 6, 1261-1266.
PDB code: 1f60
10698952 J.Y.Lee, C.Chang, H.K.Song, J.Moon, J.K.Yang, H.K.Kim, S.T.Kwon, and S.W.Suh (2000).
Crystal structure of NAD(+)-dependent DNA ligase: modular architecture and functional implications.
  EMBO J, 19, 1119-1129.
PDB codes: 1dgs 1dgt 1v9p
10866791 M.Caraglia, A.Budillon, G.Vitale, G.Lupoli, P.Tagliaferri, and A.Abbruzzese (2000).
Modulation of molecular mechanisms involved in protein synthesis machinery as a new tool for the control of cell proliferation.
  Eur J Biochem, 267, 3919-3936.  
10937867 M.Sprinzl, S.Brock, Y.Huang, P.Milovnik, M.Nanninga, M.Nesper-Brock, H.Rütthard, and K.Szkaradkiewicz (2000).
Regulation of GTPases in the bacterial translation machinery.
  Biol Chem, 381, 367-375.  
10937868 M.V.Rodnina, H.Stark, A.Savelsbergh, H.J.Wieden, D.Mohr, N.B.Matassova, F.Peske, T.Daviter, C.O.Gualerzi, and W.Wintermeyer (2000).
GTPases mechanisms and functions of translation factors on the ribosome.
  Biol Chem, 381, 377-387.  
10675317 P.Nissen, M.Kjeldgaard, and J.Nyborg (2000).
Macromolecular mimicry.
  EMBO J, 19, 489-495.  
10625477 S.E.Heffron, and F.Jurnak (2000).
Structure of an EF-Tu complex with a thiazolyl peptide antibiotic determined at 2.35 A resolution: atomic basis for GE2270A inhibition of EF-Tu.
  Biochemistry, 39, 37-45.
PDB code: 1d8t
10775275 S.Meunier, R.Spurio, M.Czisch, R.Wechselberger, M.Guenneugues, C.O.Gualerzi, and R.Boelens (2000).
Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2.
  EMBO J, 19, 1918-1926.
PDB code: 1d1n
  10739241 W.Dall'Acqua, and P.Carter (2000).
Substrate-assisted catalysis: molecular basis and biological significance.
  Protein Sci, 9, 1-9.  
10966577 X.Zhou, F.Alber, G.Folkers, G.H.Gonnet, and G.Chelvanayagam (2000).
An analysis of the helix-to-strand transition between peptides with identical sequence.
  Proteins, 41, 248-256.  
  11045624 Y.C.Cai, J.M.Bullard, N.L.Thompson, and L.L.Spremulli (2000).
Interaction of mammalian mitochondrial elongation factor EF-Tu with guanine nucleotides.
  Protein Sci, 9, 1791-1800.  
10574788 A.J.Scheidig, C.Burmester, and R.S.Goody (1999).
The pre-hydrolysis state of p21(ras) in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins.
  Structure, 7, 1311-1324.
PDB codes: 1ctq 1qra
10588048 B.Kraal, C.Lippmann, and C.Kleanthous (1999).
Translational regulation by modifications of the elongation factor Tu.
  Folia Microbiol (Praha), 44, 131-141.  
10514371 B.V.Prasad, M.E.Hardy, T.Dokland, J.Bella, M.G.Rossmann, and M.K.Estes (1999).
X-ray crystallographic structure of the Norwalk virus capsid.
  Science, 286, 287-290.
PDB code: 1ihm
10354416 D.I.Svergun (1999).
Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing.
  Biophys J, 76, 2879-2886.  
10336648 E.De Vendittis, B.S.Adinolfi, M.R.Amatruda, G.Raimo, M.Masullo, and V.Bocchini (1999).
The A26G replacement in the consensus sequence A-X-X-X-X-G-K-[T,S] of the guanine nucleotide binding site activates the intrinsic GTPase of the elongation factor 2 from the archaeon Sulfolobus solfataricus.
  Eur J Biochem, 262, 600-605.  
10371466 H.LeVine (1999).
Structural features of heterotrimeric G-protein-coupled receptors and their modulatory proteins.
  Mol Neurobiol, 19, 111-149.  
10196198 I.M.Krab, and A.Parmeggiani (1999).
Functional-structural analysis of threonine 25, a residue coordinating the nucleotide-bound magnesium in elongation factor Tu.
  J Biol Chem, 274, 11132-11138.  
10368288 J.M.Pérez, G.Siegal, J.Kriek, K.Hård, J.Dijk, G.W.Canters, and W.Möller (1999).
The solution structure of the guanine nucleotide exchange domain of human elongation factor 1beta reveals a striking resemblance to that of EF-Ts from Escherichia coli.
  Structure, 7, 217-226.
PDB code: 1b64
10445030 L.M.Rice, and A.T.Brunger (1999).
Crystal structure of the vesicular transport protein Sec17: implications for SNAP function in SNARE complex disassembly.
  Mol Cell, 4, 85-95.
PDB code: 1qqe
10371036 M.V.Rodnina, A.Savelsbergh, and W.Wintermeyer (1999).
Dynamics of translation on the ribosome: molecular mechanics of translocation.
  FEMS Microbiol Rev, 23, 317-333.  
10518715 P.M.Jones, and A.M.George (1999).
Subunit interactions in ABC transporters: towards a functional architecture.
  FEMS Microbiol Lett, 179, 187-202.  
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
10445031 R.C.Yu, R.Jahn, and A.T.Brunger (1999).
NSF N-terminal domain crystal structure: models of NSF function.
  Mol Cell, 4, 97.
PDB code: 1qcs
9873000 T.W.Dreher, O.C.Uhlenbeck, and K.S.Browning (1999).
Quantitative assessment of EF-1alpha.GTP binding to aminoacyl-tRNAs, aminoacyl-viral RNA, and tRNA shows close correspondence to the RNA binding properties of EF-Tu.
  J Biol Chem, 274, 666-672.  
10613897 T.Wendt, D.Taylor, T.Messier, K.M.Trybus, and K.A.Taylor (1999).
Visualization of head-head interactions in the inhibited state of smooth muscle myosin.
  J Cell Biol, 147, 1385-1390.  
9468489 M.Laurberg, F.Mansilla, B.F.Clark, and C.R.Knudsen (1998).
Investigation of functional aspects of the N-terminal region of elongation factor Tu from Escherichia coli using a protein engineering approach.
  J Biol Chem, 273, 4387-4391.  
9609712 N.Bilgin, M.Ehrenberg, C.Ebel, G.Zaccai, Z.Sayers, M.H.Koch, D.I.Svergun, C.Barberato, V.Volkov, P.Nissen, and J.Nyborg (1998).
Solution structure of the ternary complex between aminoacyl-tRNA, elongation factor Tu, and guanosine triphosphate.
  Biochemistry, 37, 8163-8172.  
  9436906 P.J.Farabaugh, and A.Vimaladithan (1998).
Effect of frameshift-inducing mutants of elongation factor 1alpha on programmed +1 frameshifting in yeast.
  RNA, 4, 38-46.  
9631293 S.J.Gamblin, and S.J.Smerdon (1998).
GTPase-activating proteins and their complexes.
  Curr Opin Struct Biol, 8, 195-201.  
9518480 S.Kahns, A.Lund, P.Kristensen, C.R.Knudsen, B.F.Clark, J.Cavallius, and W.C.Merrick (1998).
The elongation factor 1 A-2 isoform from rabbit: cloning of the cDNA and characterization of the protein.
  Nucleic Acids Res, 26, 1884-1890.  
9618466 X.Sun, A.L.Bognar, E.N.Baker, and C.A.Smith (1998).
Structural homologies with ATP- and folate-binding enzymes in the crystal structure of folylpolyglutamate synthetase.
  Proc Natl Acad Sci U S A, 95, 6647-6652.
PDB code: 1fgs
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.  
9249009 B.Nawrot, R.Hillenbrand, S.Limmer, N.Grillenbeck, and M.Sprinzl (1997).
Interaction of N-tosyl-L-phenylalanylchloromethane with Thermus thermophilus elongation factor Tu.
  Eur J Biochem, 247, 59-65.  
9241431 C.Chothia, T.Hubbard, S.Brenner, H.Barns, and A.Murzin (1997).
Protein folds in the all-beta and all-alpha classes.
  Annu Rev Biophys Biomol Struct, 26, 597-627.  
9315852 E.Pate, N.Naber, M.Matuska, K.Franks-Skiba, and R.Cooke (1997).
Opening of the myosin nucleotide triphosphate binding domain during the ATPase cycle.
  Biochemistry, 36, 12155-12166.  
9061031 J.Cavallius, A.P.Popkie, and W.C.Merrick (1997).
Site-directed mutants of post-translationally modified sites of yeast eEF1A using a shuttle vector containing a chromogenic switch.
  Biochim Biophys Acta, 1350, 345-358.  
9254632 J.Czworkowski, and P.B.Moore (1997).
The conformational properties of elongation factor G and the mechanism of translocation.
  Biochemistry, 36, 10327-10334.  
  9261361 J.L.Blackwell, and M.A.Brinton (1997).
Translation elongation factor-1 alpha interacts with the 3' stem-loop region of West Nile virus genomic RNA.
  J Virol, 71, 6433-6444.  
9233818 P.Fabrizio, B.Laggerbauer, J.Lauber, W.S.Lane, and R.Lührmann (1997).
An evolutionarily conserved U5 snRNP-specific protein is a GTP-binding factor closely related to the ribosomal translocase EF-2.
  EMBO J, 16, 4092-4106.  
9242920 S.R.Sprang (1997).
G protein mechanisms: insights from structural analysis.
  Annu Rev Biochem, 66, 639-678.  
9434906 S.R.Sprang (1997).
G proteins, effectors and GAPs: structure and mechanism.
  Curr Opin Struct Biol, 7, 849-856.  
9370347 T.Rattenborg, G.Nautrup Pedersen, B.F.Clark, and C.R.Knudsen (1997).
Contribution of Arg288 of Escherichia coli elongation factor Tu to translational functionality.
  Eur J Biochem, 249, 408-414.  
9253415 Y.Wang, Y.Jiang, M.Meyering-Voss, M.Sprinzl, and P.B.Sigler (1997).
Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus.
  Nat Struct Biol, 4, 650-656.
PDB code: 1aip
8805240 A.Liljas (1996).
Imprinting through molecular mimicry. Protein synthesis.
  Curr Biol, 6, 247-249.  
  8670851 A.Teplyakov, P.Sebastiao, G.Obmolova, A.Perrakis, G.S.Brush, M.J.Bessman, and K.S.Wilson (1996).
Crystal structure of bacteriophage T4 deoxynucleotide kinase with its substrates dGMP and ATP.
  EMBO J, 15, 3487-3497.
PDB codes: 1dek 1del
8663109 B.W.Poland, Z.Hou, C.Bruns, H.J.Fromm, and R.B.Honzatko (1996).
Refined crystal structures of guanine nucleotide complexes of adenylosuccinate synthetase from Escherichia coli.
  J Biol Chem, 271, 15407-15413.
PDB codes: 1hon 1hoo 1hop
8785318 C.A.Smith, and I.Rayment (1996).
Active site comparisons highlight structural similarities between myosin and other P-loop proteins.
  Biophys J, 70, 1590-1602.  
8633041 C.Borowski, M.V.Rodnina, and W.Wintermeyer (1996).
Truncated elongation factor G lacking the G domain promotes translocation of the 3' end but not of the anticodon domain of peptidyl-tRNA.
  Proc Natl Acad Sci U S A, 93, 4202-4206.  
  8978702 E.Vorstenbosch, T.Pape, M.V.Rodnina, B.Kraal, and W.Wintermeyer (1996).
The G222D mutation in elongation factor Tu inhibits the codon-induced conformational changes leading to GTPase activation on the ribosome.
  EMBO J, 15, 6766-6774.  
  8947054 F.L.Erickson, and E.M.Hannig (1996).
Ligand interactions with eukaryotic translation initiation factor 2: role of the gamma-subunit.
  EMBO J, 15, 6311-6320.  
8922379 G.Liu, J.Tang, B.T.Edmonds, J.Murray, S.Levin, and J.Condeelis (1996).
F-actin sequesters elongation factor 1alpha from interaction with aminoacyl-tRNA in a pH-dependent reaction.
  J Cell Biol, 135, 953-963.  
8939739 G.Polekhina, S.Thirup, M.Kjeldgaard, P.Nissen, C.Lippmann, and J.Nyborg (1996).
Helix unwinding in the effector region of elongation factor EF-Tu-GDP.
  Structure, 4, 1141-1151.
PDB code: 1tui
8617268 J.Blank, S.Nock, R.Kreutzer, and M.Sprinzl (1996).
Elongation factor Ts from Thermus thermophilus-- overproduction in Escherichia coli, quaternary structure and interaction with elongation factor Tu.
  Eur J Biochem, 236, 222-227.  
8916905 J.M.de Pereda, D.Leynadier, J.A.Evangelio, P.Chacón, and J.M.Andreu (1996).
Tubulin secondary structure analysis, limited proteolysis sites, and homology to FtsZ.
  Biochemistry, 35, 14203-14215.  
8768893 J.Nyborg, and M.Kjeldgaard (1996).
Elongation in bacterial protein biosynthesis.
  Curr Opin Biotechnol, 7, 369-375.  
8882578 J.Nyborg, P.Nissen, M.Kjeldgaard, S.Thirup, G.Polekhina, and B.F.Clark (1996).
Structure of the ternary complex of EF-Tu: macromolecular mimicry in translation.
  Trends Biochem Sci, 21, 81-82.  
8710841 K.A.Maegley, S.J.Admiraal, and D.Herschlag (1996).
Ras-catalyzed hydrolysis of GTP: a new perspective from model studies.
  Proc Natl Acad Sci U S A, 93, 8160-8166.  
8805530 K.Abel, and F.Jurnak (1996).
A complex profile of protein elongation: translating chemical energy into molecular movement.
  Structure, 4, 229-238.  
8939740 K.Abel, M.D.Yoder, R.Hilgenfeld, and F.Jurnak (1996).
An alpha to beta conformational switch in EF-Tu.
  Structure, 4, 1153-1159.
PDB code: 1dg1
8702777 O.Wiborg, C.Andersen, C.R.Knudsen, B.F.Clark, and J.Nyborg (1996).
Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA.
  J Biol Chem, 271, 20406-20411.  
8736554 S.al-Karadaghi, A.Aevarsson, M.Garber, J.Zheltonosova, and A.Liljas (1996).
The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange.
  Structure, 4, 555-565.
PDB code: 1dar
8916907 T.Schweins, M.Geyer, H.R.Kalbitzer, A.Wittinghofer, and A.Warshel (1996).
Linear free energy relationships in the intrinsic and GTPase activating protein-stimulated guanosine 5'-triphosphate hydrolysis of p21ras.
  Biochemistry, 35, 14225-14231.  
8706729 W.Zeidler, N.K.Schirmer, C.Egle, S.Ribeiro, R.Kreutzer, and M.Sprinzl (1996).
Limited proteolysis and amino acid replacements in the effector region of Thermus thermophilus elongation factor Tu.
  Eur J Biochem, 239, 265-271.  
8756682 Y.Jiang, S.Nock, M.Nesper, M.Sprinzl, and P.B.Sigler (1996).
Structure and importance of the dimerization domain in elongation factor Ts from Thermus thermophilus.
  Biochemistry, 35, 10269-10278.
PDB code: 1tfe
  8771196 Y.Zhang, C.S.Bond, S.Bailey, M.L.Cunningham, A.H.Fairlamb, and W.N.Hunter (1996).
The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 A resolution.
  Protein Sci, 5, 52-61.
PDB code: 1aog
8749358 A.Liljas, and M.Garber (1995).
Ribosomal proteins and elongation factors.
  Curr Opin Struct Biol, 5, 721-727.  
  8722034 B.Kraal, L.A.Zeef, J.R.Mesters, K.Boon, E.L.Vorstenbosch, L.Bosch, P.H.Anborgh, A.Parmeggiani, and R.Hilgenfeld (1995).
Antibiotic resistance mechanisms of mutant EF-Tu species in Escherichia coli.
  Biochem Cell Biol, 73, 1167-1177.  
7782317 C.Alexander, N.Bilgin, C.Lindschau, J.R.Mesters, B.Kraal, R.Hilgenfeld, V.A.Erdmann, and C.Lippmann (1995).
Phosphorylation of elongation factor Tu prevents ternary complex formation.
  J Biol Chem, 270, 14541-14547.  
7883001 C.R.Knudsen, I.V.Kjaersgård, O.Wiborg, and B.F.Clark (1995).
Mutation of the conserved Gly94 and Gly126 in elongation factor Tu from Escherichia coli. Elucidation of their structural and functional roles.
  Eur J Biochem, 228, 176-183.  
  7774582 D.R.Dorris, F.L.Erickson, and E.M.Hannig (1995).
Mutations in GCD11, the structural gene for eIF-2 gamma in yeast, alter translational regulation of GCN4 and the selection of the start site for protein synthesis.
  EMBO J, 14, 2239-2249.  
7749921 G.Casari, C.Sander, and A.Valencia (1995).
A method to predict functional residues in proteins.
  Nat Struct Biol, 2, 171-178.  
7883002 I.V.Kjaersgård, C.R.Knudsen, and O.Wiborg (1995).
Mutation of the conserved Gly83 and Gly94 in Escherichia coli elongation factor Tu. Indication of structural pivots.
  Eur J Biochem, 228, 184-190.  
7730301 J.M.Zhong, M.C.Chen-Hwang, and Y.W.Hwang (1995).
Switching nucleotide specificity of Ha-Ras p21 by a single amino acid substitution at aspartate 119.
  J Biol Chem, 270, 10002-10007.  
7543023 K.L.Gunderson, and R.R.Kopito (1995).
Conformational states of CFTR associated with channel gating: the role ATP binding and hydrolysis.
  Cell, 82, 231-239.  
  7781613 M.V.Rodnina, R.Fricke, L.Kuhn, and W.Wintermeyer (1995).
Codon-dependent conformational change of elongation factor Tu preceding GTP hydrolysis on the ribosome.
  EMBO J, 14, 2613-2619.  
  8722040 M.V.Rodnina, T.Pape, R.Fricke, and W.Wintermeyer (1995).
Elongation factor Tu, a GTPase triggered by codon recognition on the ribosome: mechanism and GTP consumption.
  Biochem Cell Biol, 73, 1221-1227.  
7719851 R.Hilgenfeld (1995).
How do the GTPases really work?
  Nat Struct Biol, 2, 3-6.  
8749370 R.Hilgenfeld (1995).
Regulatory GTPases.
  Curr Opin Struct Biol, 5, 810-817.  
8529632 S.Nock, N.Grillenbeck, M.R.Ahmadian, S.Ribeiro, R.Kreutzer, and M.Sprinzl (1995).
Properties of isolated domains of the elongation factor Tu from Thermus thermophilus HB8.
  Eur J Biochem, 234, 132-139.  
7719852 T.Schweins, M.Geyer, K.Scheffzek, A.Warshel, H.R.Kalbitzer, and A.Wittinghofer (1995).
Substrate-assisted catalysis as a mechanism for GTP hydrolysis of p21ras and other GTP-binding proteins.
  Nat Struct Biol, 2, 36-44.  
7758452 W.Zeidler, C.Egle, S.Ribeiro, A.Wagner, V.Katunin, R.Kreutzer, M.Rodnina, W.Wintermeyer, and M.Sprinzl (1995).
Site-directed mutagenesis of Thermus thermophilus elongation factor Tu. Replacement of His85, Asp81 and Arg300.
  Eur J Biochem, 229, 596-604.  
  8070397 A.AEvarsson, E.Brazhnikov, M.Garber, J.Zheltonosova, Y.Chirgadze, S.al-Karadaghi, L.A.Svensson, and A.Liljas (1994).
Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus.
  EMBO J, 13, 3669-3677.
PDB code: 1elo
8048158 A.Weijland, and A.Parmeggiani (1994).
Why do two EF-Tu molecules act in the elongation cycle of protein biosynthesis?
  Trends Biochem Sci, 19, 188-193.  
8293457 A.Wittinghofer (1994).
The structure of transducin G alpha t: more to view than just ras.
  Cell, 76, 201-204.  
8143728 C.Andersen, and O.Wiborg (1994).
Escherichia coli elongation-factor-Tu mutants with decreased affinity for aminoacyl-tRNA.
  Eur J Biochem, 220, 739-744.  
7937899 C.Kleuss, A.S.Raw, E.Lee, S.R.Sprang, and A.G.Gilman (1994).
Mechanism of GTP hydrolysis by G-protein alpha subunits.
  Proc Natl Acad Sci U S A, 91, 9828-9831.  
7812711 F.Jurnak (1994).
The ABC of EF-G.
  Structure, 2, 785-788.  
  8070396 J.Czworkowski, J.Wang, T.A.Steitz, and P.B.Moore (1994).
The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution.
  EMBO J, 13, 3661-3668.
PDB codes: 1efg 2efg
  7525272 J.R.Mesters, L.A.Zeef, R.Hilgenfeld, J.M.de Graaf, B.Kraal, and L.Bosch (1994).
The structural and functional basis for the kirromycin resistance of mutant EF-Tu species in Escherichia coli.
  EMBO J, 13, 4877-4885.  
  7957075 L.A.Zeef, L.Bosch, P.H.Anborgh, R.Cetin, A.Parmeggiani, and R.Hilgenfeld (1994).
Pulvomycin-resistant mutants of E.coli elongation factor Tu.
  EMBO J, 13, 5113-5120.  
8073502 M.Sprinzl (1994).
Elongation factor Tu: a regulatory GTPase with an integrated effector.
  Trends Biochem Sci, 19, 245-250.  
7922378 T.Schweins, and A.Wittinghofer (1994).
GTP-binding proteins. Structures, interactions and relationships.
  Curr Biol, 4, 547-550.  
15335821 A.Wittinghofer (1993).
From EF-Tu to p21ras and back again.
  Curr Biol, 3, 874-876.  
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