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PDBsum entry 1fts
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Signal recognition particle receptor PDB id
1fts

 

 

 

 

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Contents
Protein chain
295 a.a. *
* Residue conservation analysis
PDB id:
1fts
Name: Signal recognition particle receptor
Title: Signal recognition particle receptor from e. Coli
Structure: Ftsy. Chain: a. Fragment: ng-domain residues 197 - 497. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Cellular_location: cytoplasm, cytoplasma membrane. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Resolution:
2.20Å     R-factor:   0.222     R-free:   0.280
Authors: G.Montoya,C.Svensson,J.Luirink,I.Sinning
Key ref: G.Montoya et al. (1997). Crystal structure of the NG domain from the signal-recognition particle receptor FtsY. Nature, 385, 365-368. PubMed id: 9002525
Date:
20-Nov-96     Release date:   20-May-98    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P10121  (FTSY_ECOLI) -  Signal recognition particle receptor FtsY from Escherichia coli (strain K12)
Seq:
Struc: 		497 a.a.
295 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.6.5.4  - signal-recognition-particle GTPase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: GTP + H2O = GDP + phosphate + H+
GTP
 + H2O
 = GDP
 + phosphate
 + H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Nature 385:365-368 (1997)
PubMed id: 9002525  
 
 
Crystal structure of the NG domain from the signal-recognition particle receptor FtsY.
G.Montoya, C.Svensson, J.Luirink, I.Sinning.
 
  ABSTRACT  
 
Newly synthesized proteins destined either for secretion or incorporation into membranes are targeted to the membrane translocation machinery by a ubiquitous system consisting of a signal-recognition particle (SRP) and its receptor. Both the SRP receptor and the protein within the SRP that binds the signal sequence contain GTPases. These two proteins, together with the RNA component of the SRP, form a complex and thereby regulate each other's GTPase activity. Here we report the structure of the GTPase-containing portion of FtsY, the functional homologue of the SRP receptor of Escherichia coli, at 2.2 A resolution without bound nucleotide. This so-called NG domain displays similarities to the Ras-related GTPases, as well as features unique to the SRP-type GTPases, such as a separate amino-terminal domain, an insertion within the p21ras (Ras) effector domain, and a wide-open GTP-binding region. The structure explains the low affinity of FtsY for GTP, and suggests rearrangements that may occur on nucleotide binding. It also identifies regions potentially involved in the transmission of signals between domains and in interactions with regulatory proteins.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22056770 G.Bange, N.Kümmerer, P.Grudnik, R.Lindner, G.Petzold, D.Kressler, E.Hurt, K.Wild, and I.Sinning (2011).
Structural basis for the molecular evolution of SRP-GTPase activation by protein.
  Nat Struct Mol Biol, 18, 1376-1380.
PDB code: 3syn
21151118 L.F.Estrozi, D.Boehringer, S.O.Shan, N.Ban, and C.Schaffitzel (2011).
Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor.
  Nat Struct Mol Biol, 18, 88-90.
PDB code: 2xkv
  21465554 M.J.Yang, and X.Zhang (2011).
Molecular dynamics simulations reveal structural coordination of Ffh-FtsY heterodimer toward GTPase activation.
  Proteins, 79, 1774-1785.  
21276251 N.Pawlowski, A.Khaminets, J.P.Hunn, N.Papic, A.Schmidt, R.C.Uthaiah, R.Lange, G.Vopper, S.Martens, E.Wolf, and J.C.Howard (2011).
The activation mechanism of Irga6, an interferon-inducible GTPase contributing to mouse resistance against Toxoplasma gondii.
  BMC Biol, 9, 7.  
20123128 K.W.Hung, Y.W.Chang, E.T.Eng, J.H.Chen, Y.C.Chen, Y.J.Sun, C.D.Hsiao, G.Dong, K.A.Spasov, V.M.Unger, and T.H.Huang (2010).
Structural fold, conservation and Fe(II) binding of the intracellular domain of prokaryote FeoB.
  J Struct Biol, 170, 501-512.
PDB codes: 2wia 2wib 2wic 3k53
20146389 M.E.Reinau, I.B.Thøgersen, J.J.Enghild, K.L.Nielsen, and D.E.Otzen (2010).
The diversity of FtsY-lipid interactions.
  Biopolymers, 93, 595-606.  
20544960 M.Yang, X.Zhang, and K.Han (2010).
Molecular dynamics simulation of SRP GTPases: towards an understanding of the complex formation from equilibrium fluctuations.
  Proteins, 78, 2222-2237.  
20204450 S.J.Facey, and A.Kuhn (2010).
Biogenesis of bacterial inner-membrane proteins.
  Cell Mol Life Sci, 67, 2343-2362.  
20733058 V.Q.Lam, D.Akopian, M.Rome, D.Henningsen, and S.O.Shan (2010).
Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting.
  J Cell Biol, 190, 623-635.  
19675567 A.Mateja, A.Szlachcic, M.E.Downing, M.Dobosz, M.Mariappan, R.S.Hegde, and R.J.Keenan (2009).
The structural basis of tail-anchored membrane protein recognition by Get3.
  Nature, 461, 361-366.
PDB codes: 2woj 2woo
19706470 C.J.Suloway, J.W.Chartron, M.Zaslaver, and W.M.Clemons (2009).
Model for eukaryotic tail-anchored protein binding based on the structure of Get3.
  Proc Natl Acad Sci U S A, 106, 14849-14854.
PDB codes: 3ibg 3idq
19948960 G.Bozkurt, G.Stjepanovic, F.Vilardi, S.Amlacher, K.Wild, G.Bange, V.Favaloro, K.Rippe, E.Hurt, B.Dobberstein, and I.Sinning (2009).
Structural insights into tail-anchored protein binding and membrane insertion by Get3.
  Proc Natl Acad Sci U S A, 106, 21131-21136.
PDB codes: 3iqw 3iqx
19029307 I.A.Buskiewicz, J.Jöckel, M.V.Rodnina, and W.Wintermeyer (2009).
Conformation of the signal recognition particle in ribosomal targeting complexes.
  RNA, 15, 44-54.  
19558326 P.Grudnik, G.Bange, and I.Sinning (2009).
Protein targeting by the signal recognition particle.
  Biol Chem, 390, 775-782.  
19587121 P.Jaru-Ampornpan, T.X.Nguyen, and S.O.Shan (2009).
A distinct mechanism to achieve efficient signal recognition particle (SRP)-SRP receptor interaction by the chloroplast srp pathway.
  Mol Biol Cell, 20, 3965-3973.  
19469550 S.O.Shan, S.L.Schmid, and X.Zhang (2009).
Signal recognition particle (SRP) and SRP receptor: a new paradigm for multistate regulatory GTPases.
  Biochemistry, 48, 6696-6704.  
18078384 A.J.Driessen, and N.Nouwen (2008).
Protein translocation across the bacterial cytoplasmic membrane.
  Annu Rev Biochem, 77, 643-667.  
18068722 E.T.Eng, A.R.Jalilian, K.A.Spasov, and V.M.Unger (2008).
Characterization of a novel prokaryotic GDP dissociation inhibitor domain from the G protein coupled membrane protein FeoB.
  J Mol Biol, 375, 1086-1097.  
18978942 P.F.Egea, H.Tsuruta, G.P.de Leon, J.Napetschnig, P.Walter, and R.M.Stroud (2008).
Structures of the signal recognition particle receptor from the archaeon Pyrococcus furiosus: implications for the targeting step at the membrane.
  PLoS ONE, 3, e3619.
PDB codes: 3dm9 3dmd 3e70
19172744 S.B.Neher, N.Bradshaw, S.N.Floor, J.D.Gross, and P.Walter (2008).
SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.
  Nat Struct Mol Biol, 15, 916-923.  
18931411 U.D.Ramirez, P.J.Focia, and D.M.Freymann (2008).
Nucleotide-binding flexibility in ultrahigh-resolution structures of the SRP GTPase Ffh.
  Acta Crystallogr D Biol Crystallogr, 64, 1043-1053.
PDB codes: 2c03 2c04
17622352 C.L.Reyes, E.Rutenber, P.Walter, and R.M.Stroud (2007).
X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates.
  PLoS ONE, 2, e607.
PDB codes: 2q9a 2q9b 2q9c
  17565194 G.Bange, G.Petzold, K.Wild, and I.Sinning (2007).
Expression, purification and preliminary crystallographic characterization of FlhF from Bacillus subtilis.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 449-451.  
17699634 G.Bange, G.Petzold, K.Wild, R.O.Parlitz, and I.Sinning (2007).
The crystal structure of the third signal-recognition particle GTPase FlhF reveals a homodimer with bound GTP.
  Proc Natl Acad Sci U S A, 104, 13621-13625.
PDB codes: 2px0 2px3
17184999 J.Gawronski-Salerno, and D.M.Freymann (2007).
Structure of the GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsY.
  J Struct Biol, 158, 122-128.
PDB code: 2j7p
17186523 J.Gawronski-Salerno, J.S.Coon, P.J.Focia, and D.M.Freymann (2007).
X-ray structure of the T. aquaticus FtsY:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPases.
  Proteins, 66, 984-995.
PDB code: 2iyl
17726013 L.Bahari, R.Parlitz, A.Eitan, G.Stjepanovic, E.S.Bochkareva, I.Sinning, and E.Bibi (2007).
Membrane targeting of ribosomes and their release require distinct and separable functions of FtsY.
  J Biol Chem, 282, 32168-32175.  
17475780 P.Jaru-Ampornpan, S.Chandrasekar, and S.O.Shan (2007).
Efficient interaction between two GTPases allows the chloroplast SRP pathway to bypass the requirement for an SRP RNA.
  Mol Biol Cell, 18, 2636-2645.  
17726012 R.Parlitz, A.Eitan, G.Stjepanovic, L.Bahari, G.Bange, E.Bibi, and I.Sinning (2007).
Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix.
  J Biol Chem, 282, 32176-32184.  
17682051 S.O.Shan, S.Chandrasekar, and P.Walter (2007).
Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation.
  J Cell Biol, 178, 611-620.  
17126854 S.Wu, A.Ke, and J.A.Doudna (2007).
A fast and efficient procedure to produce scFvs specific for large macromolecular complexes.
  J Immunol Methods, 318, 95.  
16469117 K.Römisch, F.W.Miller, B.Dobberstein, and S.High (2006).
Human autoantibodies against the 54 kDa protein of the signal recognition particle block function at multiple stages.
  Arthritis Res Ther, 8, R39.  
17139088 U.D.Ramirez, and D.M.Freymann (2006).
Analysis of protein hydration in ultrahigh-resolution structures of the SRP GTPase Ffh.
  Acta Crystallogr D Biol Crystallogr, 62, 1520-1534.
PDB codes: 2j45 2j46
15923378 I.Buskiewicz, A.Kubarenko, F.Peske, M.V.Rodnina, and W.Wintermeyer (2005).
Domain rearrangement of SRP protein Ffh upon binding 4.5S RNA and the SRP receptor FtsY.
  RNA, 11, 947-957.  
14749771 E.C.Mandon, and R.Gilmore (2004).
GTPase twins in the SRP family.
  Nat Struct Mol Biol, 11, 115-116.  
15546976 F.Chu, S.O.Shan, D.T.Moustakas, F.Alber, P.F.Egea, R.M.Stroud, P.Walter, and A.L.Burlingame (2004).
Unraveling the interface of signal recognition particle and its receptor by using chemical cross-linking and tandem mass spectrometry.
  Proc Natl Acad Sci U S A, 101, 16454-16459.  
15189152 J.A.Doudna, and R.T.Batey (2004).
Structural insights into the signal recognition particle.
  Annu Rev Biochem, 73, 539-557.  
15228518 K.Wild, K.R.Rosendal, and I.Sinning (2004).
A structural step into the SRP cycle.
  Mol Microbiol, 53, 357-363.  
15523481 K.Wild, M.Halic, I.Sinning, and R.Beckmann (2004).
SRP meets the ribosome.
  Nat Struct Mol Biol, 11, 1049-1053.  
14724630 P.F.Egea, S.O.Shan, J.Napetschnig, D.F.Savage, P.Walter, and R.M.Stroud (2004).
Substrate twinning activates the signal recognition particle and its receptor.
  Nature, 427, 215-221.
PDB code: 1rj9
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
14726591 P.J.Focia, I.V.Shepotinovskaya, J.A.Seidler, and D.M.Freymann (2004).
Heterodimeric GTPase core of the SRP targeting complex.
  Science, 303, 373-377.
PDB code: 1okk
15383838 S.O.Shan, R.M.Stroud, and P.Walter (2004).
Mechanism of association and reciprocal activation of two GTPases.
  PLoS Biol, 2, e320.  
15030489 T.Lichi, G.Ring, and J.Eichler (2004).
Membrane binding of SRP pathway components in the halophilic archaea Haloferax volcanii.
  Eur J Biochem, 271, 1382-1390.  
14501130 I.V.Shepotinovskaya, P.J.Focia, and D.M.Freymann (2003).
Crystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY.
  Acta Crystallogr D Biol Crystallogr, 59, 1834-1837.  
12682065 K.McLuskey, J.A.Harrison, A.W.Schuttelkopf, D.H.Boxer, and W.N.Hunter (2003).
Insight into the role of Escherichia coli MobB in molybdenum cofactor biosynthesis based on the high resolution crystal structure.
  J Biol Chem, 278, 23706-23713.
PDB code: 1np6
12853463 K.Nagai, C.Oubridge, A.Kuglstatter, E.Menichelli, C.Isel, and L.Jovine (2003).
Structure, function and evolution of the signal recognition particle.
  EMBO J, 22, 3479-3485.  
14657338 K.R.Rosendal, K.Wild, G.Montoya, and I.Sinning (2003).
Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication.
  Proc Natl Acad Sci U S A, 100, 14701-14706.
PDB codes: 1qzw 1qzx
12663860 S.O.Shan, and P.Walter (2003).
Induced nucleotide specificity in a GTPase.
  Proc Natl Acad Sci U S A, 100, 4480-4485.  
12702815 S.Q.Gu, F.Peske, H.J.Wieden, M.V.Rodnina, and W.Wintermeyer (2003).
The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome.
  RNA, 9, 566-573.  
12654246 T.Schwartz, and G.Blobel (2003).
Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor.
  Cell, 112, 793-803.
PDB code: 1nrj
  15803656 C.Zwieb, and J.Eichler (2002).
Getting on target: the archaeal signal recognition particle.
  Archaea, 1, 27-34.  
12429099 J.Buglino, V.Shen, P.Hakimian, and C.D.Lima (2002).
Structural and biochemical analysis of the Obg GTP binding protein.
  Structure, 10, 1581-1592.
PDB code: 1lnz
12244113 L.Liu, X.H.Liang, S.Uliel, R.Unger, E.Ullu, and S.Michaeli (2002).
RNA interference of signal peptide-binding protein SRP54 elicits deleterious effects and protein sorting defects in trypanosomes.
  J Biol Chem, 277, 47348-47357.  
11713194 A.A.Herskovits, A.Seluanov, R.Rajsbaum, C.M.ten Hagen-Jongman, T.Henrichs, E.S.Bochkareva, G.J.Phillips, F.J.Probst, T.Nakae, M.Ehrmann, J.Luirink, and E.Bibi (2001).
Evidence for coupling of membrane targeting and function of the signal recognition particle (SRP) receptor FtsY.
  EMBO Rep, 2, 1040-1046.  
11689422 H.H.Niemann, M.L.Knetsch, A.Scherer, D.J.Manstein, and F.J.Kull (2001).
Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms.
  EMBO J, 20, 5813-5821.
PDB codes: 1jwy 1jx2
11233986 J.R.Jagath, N.B.Matassova, E.de Leeuw, J.M.Warnecke, G.Lentzen, M.V.Rodnina, J.Luirink, and W.Wintermeyer (2001).
Important role of the tetraloop region of 4.5S RNA in SRP binding to its receptor FtsY.
  RNA, 7, 293-301.  
11350037 O.Weichenrieder, C.Stehlin, U.Kapp, D.E.Birse, P.A.Timmins, K.Strub, and S.Cusack (2001).
Hierarchical assembly of the Alu domain of the mammalian signal recognition particle.
  RNA, 7, 731-740.  
11735405 P.Peluso, S.O.Shan, S.Nock, D.Herschlag, and P.Walter (2001).
Role of SRP RNA in the GTPase cycles of Ffh and FtsY.
  Biochemistry, 40, 15224-15233.  
11395422 R.J.Keenan, D.M.Freymann, R.M.Stroud, and P.Walter (2001).
The signal recognition particle.
  Annu Rev Biochem, 70, 755-775.  
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
11331598 T.A.Fulga, I.Sinning, B.Dobberstein, and M.R.Pool (2001).
SRbeta coordinates signal sequence release from SRP with ribosome binding to the translocon.
  EMBO J, 20, 2338-2347.  
11726508 Y.Lu, H.Y.Qi, J.B.Hyndman, N.D.Ulbrandt, A.Teplyakov, N.Tomasevic, and H.D.Bernstein (2001).
Evidence for a novel GTPase priming step in the SRP protein targeting pathway.
  EMBO J, 20, 6724-6734.  
11123669 A.A.Herskovits, E.S.Bochkareva, and E.Bibi (2000).
New prospects in studying the bacterial signal recognition particle pathway.
  Mol Microbiol, 38, 927-939.  
10675322 E.de Leeuw, K.te Kaat, C.Moser, G.Menestrina, R.Demel, B.de Kruijff, B.Oudega, J.Luirink, and I.Sinning (2000).
Anionic phospholipids are involved in membrane association of FtsY and stimulate its GTPase activity.
  EMBO J, 19, 531-541.  
10801496 G.Montoya, K.Kaat, R.Moll, G.Schäfer, and I.Sinning (2000).
The crystal structure of the conserved GTPase of SRP54 from the archaeon Acidianus ambivalens and its comparison with related structures suggests a model for the SRP-SRP receptor complex.
  Structure, 8, 515-525.
PDB codes: 1j8m 1j8y
  11048650 J.Kim, and D.A.Kendall (2000).
Sec-dependent protein export and the involvement of the molecular chaperone SecB.
  Cell Stress Chaperones, 5, 267-275.  
10834842 P.Peluso, D.Herschlag, S.Nock, D.M.Freymann, A.E.Johnson, and P.Walter (2000).
Role of 4.5S RNA in assembly of the bacterial signal recognition particle with its receptor.
  Science, 288, 1640-1643.  
10678824 R.T.Batey, R.P.Rambo, L.Lucast, B.Rha, and J.A.Doudna (2000).
Crystal structure of the ribonucleoprotein core of the signal recognition particle.
  Science, 287, 1232-1239.
PDB code: 1dul
10684931 S.H.Bhuiyan, K.Gowda, H.Hotokezaka, and C.Zwieb (2000).
Assembly of archaeal signal recognition particle from recombinant components.
  Nucleic Acids Res, 28, 1365-1373.  
10944345 T.Gariani, and E.Sauer-Eriksson (2000).
Crystallization and preliminary X-ray diffraction studies of the signal recognition particle receptor FtsY from Mycoplasma mycoides.
  Acta Crystallogr D Biol Crystallogr, 56, 1030-1032.  
10931860 W.A.Prinz, L.Grzyb, M.Veenhuis, J.A.Kahana, P.A.Silver, and T.A.Rapoport (2000).
Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisiae.
  J Cell Biol, 150, 461-474.  
10611978 A.E.Johnson, and M.A.van Waes (1999).
The translocon: a dynamic gateway at the ER membrane.
  Annu Rev Cell Dev Biol, 15, 799-842.  
10459008 G.Bacher, M.Pool, and B.Dobberstein (1999).
The ribosome regulates the GTPase of the beta-subunit of the signal recognition particle receptor.
  J Cell Biol, 146, 723-730.  
10531505 G.Montoya, K.te Kaat, R.Moll, G.Schäfer, and I.Sinning (1999).
Crystallization and preliminary x-ray diffraction studies on the conserved GTPase domain of the signal recognition particle from Acidianus ambivalens.
  Acta Crystallogr D Biol Crystallogr, 55, 1949-1951.  
10559196 J.S.Millman, and D.W.Andrews (1999).
A site-specific, membrane-dependent cleavage event defines the membrane binding domain of FtsY.
  J Biol Chem, 274, 33227-33234.  
  10338025 K.Gowda, W.M.Clemons, C.Zwieb, and S.D.Black (1999).
Expression, purification, and crystallography of the conserved methionine-rich domain of human signal recognition particle 54 kDa protein.
  Protein Sci, 8, 1144-1151.  
  10066835 P.Fekkes, and A.J.Driessen (1999).
Protein targeting to the bacterial cytoplasmic membrane.
  Microbiol Mol Biol Rev, 63, 161-173.  
10607673 R.M.Stroud, and P.Walter (1999).
Signal sequence recognition and protein targeting.
  Curr Opin Struct Biol, 9, 754-759.  
9914525 R.Moll, S.Schmidtke, and G.Schäfer (1999).
Domain structure, GTP-hydrolyzing activity and 7S RNA binding of Acidianus ambivalens ffh-homologous protein suggest an SRP-like complex in archaea.
  Eur J Biochem, 259, 441-448.  
10411886 X.Chen, D.L.Court, and X.Ji (1999).
Crystal structure of ERA: a GTPase-dependent cell cycle regulator containing an RNA binding motif.
  Proc Natl Acad Sci U S A, 96, 8396-8401.
PDB code: 1ega
9778518 H.D.Bernstein (1998).
Protein targeting: getting into the groove.
  Curr Biol, 8, R715-R718.  
9695947 R.J.Keenan, D.M.Freymann, P.Walter, and R.M.Stroud (1998).
Crystal structure of the signal sequence binding subunit of the signal recognition particle.
  Cell, 94, 181-191.
PDB code: 2ffh
  9563818 R.Jaenicke (1998).
Protein self-organization in vitro and in vivo: partitioning between physical biochemistry and cell biology.
  Biol Chem, 379, 237-243.  
9679135 S.C.Ogg, W.P.Barz, and P.Walter (1998).
A functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit.
  J Cell Biol, 142, 341-354.  
9177162 A.Zelazny, A.Seluanov, A.Cooper, and E.Bibi (1997).
The NG domain of the prokaryotic signal recognition particle receptor, FtsY, is fully functional when fused to an unrelated integral membrane polypeptide.
  Proc Natl Acad Sci U S A, 94, 6025-6029.  
9326611 C.Moser, O.Mol, R.S.Goody, and I.Sinning (1997).
The signal recognition particle receptor of Escherichia coli (FtsY) has a nucleotide exchange factor built into the GTPase domain.
  Proc Natl Acad Sci U S A, 94, 11339-11344.  
9182753 J.S.Millman, and D.W.Andrews (1997).
Switching the model: a concerted mechanism for GTPases in protein targeting.
  Cell, 89, 673-676.  
9353225 M.Sakaguchi (1997).
Eukaryotic protein secretion.
  Curr Opin Biotechnol, 8, 595-601.  
9659905 N.Zheng, and L.M.Gierasch (1997).
Domain interactions in E. coli SRP: stabilization of M domain by RNA is required for effective signal sequence modulation of NG domain.
  Mol Cell, 1, 79-87.  
9182758 P.J.Rapiejko, and R.Gilmore (1997).
Empty site forms of the SRP54 and SR alpha GTPases mediate targeting of ribosome-nascent chain complexes to the endoplasmic reticulum.
  Cell, 89, 703-713.  
9434906 S.R.Sprang (1997).
G proteins, effectors and GAPs: structure and mechanism.
  Curr Opin Struct Biol, 7, 849-856.  
9305630 T.Powers, and P.Walter (1997).
Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor.
  EMBO J, 16, 4880-4886.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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