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PDBsum entry 2chf

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protein links
Signal transduction protein PDB id
2chf
Jmol
Contents
Protein chain
128 a.a. *
Waters ×95
* Residue conservation analysis
PDB id:
2chf
Name: Signal transduction protein
Title: Structure of the mg2+-bound form of chey and the mechanism of phosphoryl transfer in bacterial chemotaxis
Structure: Chey. Chain: a. Engineered: yes
Source: Salmonella typhimurium. Organism_taxid: 602
Resolution:
1.80Å     R-factor:   0.180    
Authors: A.Stock,E.Martinez-Hackert,B.Rasmussen,A.West,J.Stock, D.Ringe,G.Petsko
Key ref:
A.M.Stock et al. (1993). Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis. Biochemistry, 32, 13375-13380. PubMed id: 8257674 DOI: 10.1021/bi00212a001
Date:
17-Jan-94     Release date:   30-Apr-94    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0A2D5  (CHEY_SALTY) -  Chemotaxis protein CheY
Seq:
Struc:
129 a.a.
128 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     intracellular signal transduction   4 terms 
  Biochemical function     two-component response regulator activity     2 terms  

 

 
DOI no: 10.1021/bi00212a001 Biochemistry 32:13375-13380 (1993)
PubMed id: 8257674  
 
 
Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis.
A.M.Stock, E.Martinez-Hackert, B.F.Rasmussen, A.H.West, J.B.Stock, D.Ringe, G.A.Petsko.
 
  ABSTRACT  
 
The response regulator protein of bacterial chemotaxis, CheY, is representative of a large family of signal transduction proteins that function as phosphorylation-activated switches to regulate the activities of associated effector domains. These regulators catalyze the metal ion-dependent phosphoryl transfer and dephosphorylation reactions that control the effector activities. The crystal structures of Salmonella typhimurium CheY with and without Mg2+ bound at the active site have been determined and refined at 1.8-A resolution. While the overall structures of metal-bound and metal-free CheY are similar, significant rearrangements occur within the active site involving the three most highly conserved residues of the response regulator family. Conservation of the cluster of carboxylate side chains at the active site of response regulator domains can be rationalized in terms of their role in coordinating the catalytically essential divalent metal ion. The Mg2+ coordination geometry provides insights to the mechanism of phosphoryl transfer.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20161720 C.H.Bell, S.L.Porter, A.Strawson, D.I.Stuart, and J.P.Armitage (2010).
Using structural information to change the phosphotransfer specificity of a two-component chemotaxis signalling complex.
  PLoS Biol, 8, e1000306.
PDB codes: 3kyi 3kyj
20735776 J.Herrou, R.Foreman, A.Fiebig, and S.Crosson (2010).
A structural model of anti-anti-σ inhibition by a two-component receiver domain: the PhyR stress response regulator.
  Mol Microbiol, 78, 290-304.
PDB code: 3n0r
20809990 J.V.Møller, C.Olesen, A.M.Winther, and P.Nissen (2010).
The sarcoplasmic Ca2+-ATPase: design of a perfect chemi-osmotic pump.
  Q Rev Biophys, 43, 501-566.  
20213047 K.Dong, Q.Li, C.Liu, Y.Zhang, G.Zhao, and X.Guo (2010).
Cloning and characterization of three cheB genes in Leptospira interrogans.
  Acta Biochim Biophys Sin (Shanghai), 42, 216-223.  
20133180 R.E.Silversmith (2010).
Auxiliary phosphatases in two-component signal transduction.
  Curr Opin Microbiol, 13, 177-183.  
19575571 R.Gao, and A.M.Stock (2009).
Biological insights from structures of two-component proteins.
  Annu Rev Microbiol, 63, 133-154.  
19304952 X.J.He, K.E.Mulford, and J.S.Fassler (2009).
Oxidative stress function of the Saccharomyces cerevisiae Skn7 receiver domain.
  Eukaryot Cell, 8, 768-778.  
19646451 Y.Pazy, A.C.Wollish, S.A.Thomas, P.J.Miller, E.J.Collins, R.B.Bourret, and R.E.Silversmith (2009).
Matching biochemical reaction kinetics to the timescales of life: structural determinants that influence the autodephosphorylation rate of response regulator proteins.
  J Mol Biol, 392, 1205-1220.
PDB codes: 3f7n 3fft 3ffw 3ffx 3fgz
18353359 G.Wisedchaisri, M.Wu, D.R.Sherman, and W.G.Hol (2008).
Crystal structures of the response regulator DosR from Mycobacterium tuberculosis suggest a helix rearrangement mechanism for phosphorylation activation.
  J Mol Biol, 378, 227-242.
PDB codes: 3c3w 3c57
17998207 R.E.Silversmith, M.D.Levin, E.Schilling, and R.B.Bourret (2008).
Kinetic characterization of catalysis by the chemotaxis phosphatase CheZ. Modulation of activity by the phosphorylated CheY substrate.
  J Biol Chem, 283, 756-765.  
18557815 S.A.Thomas, J.A.Brewster, and R.B.Bourret (2008).
Two variable active site residues modulate response regulator phosphoryl group stability.
  Mol Microbiol, 69, 453-465.  
18076904 X.Zhao, D.M.Copeland, A.S.Soares, and A.H.West (2008).
Crystal structure of a complex between the phosphorelay protein YPD1 and the response regulator domain of SLN1 bound to a phosphoryl analog.
  J Mol Biol, 375, 1141-1151.
PDB code: 2r25
17172298 M.H.Knaggs, F.R.Salsbury, M.H.Edgell, and J.S.Fetrow (2007).
Insights into correlated motions and long-range interactions in CheY derived from molecular dynamics simulations.
  Biophys J, 92, 2062-2079.  
17511470 N.Friedland, T.R.Mack, M.Yu, L.W.Hung, T.C.Terwilliger, G.S.Waldo, and A.M.Stock (2007).
Domain orientation in the inactive response regulator Mycobacterium tuberculosis MtrA provides a barrier to activation.
  Biochemistry, 46, 6733-6743.
PDB code: 2gwr
17433693 R.Gao, T.R.Mack, and A.M.Stock (2007).
Bacterial response regulators: versatile regulatory strategies from common domains.
  Trends Biochem Sci, 32, 225-234.  
17050923 C.M.Dyer, and F.W.Dahlquist (2006).
Switched or not?: the structure of unphosphorylated CheY bound to the N terminus of FliM.
  J Bacteriol, 188, 7354-7363.
PDB code: 2b1j
16877509 H.Yang, L.Hu, J.Shi, and J.Cui (2006).
Tuning magnesium sensitivity of BK channels by mutations.
  Biophys J, 91, 2892-2900.  
16740923 M.Y.Galperin (2006).
Structural classification of bacterial response regulators: diversity of output domains and domain combinations.
  J Bacteriol, 188, 4169-4182.  
16950782 S.L.Porter, G.H.Wadhams, A.C.Martin, E.D.Byles, D.E.Lancaster, and J.P.Armitage (2006).
The CheYs of Rhodobacter sphaeroides.
  J Biol Chem, 281, 32694-32704.  
15741343 T.J.Lowery, M.Doucleff, E.J.Ruiz, S.M.Rubin, A.Pines, and D.E.Wemmer (2005).
Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR.
  Protein Sci, 14, 848-855.
PDB code: 1zdm
14563853 A.C.Harrod, X.Yang, M.Junker, and L.Reitzer (2004).
Evidence for a second interaction between the regulatory amino-terminal and central output domains of the response regulator NtrC (nitrogen regulator I) in Escherichia coli.
  J Biol Chem, 279, 2350-2359.  
15039551 D.Mukhopadhyay, U.Sen, J.Zapf, and K.I.Varughese (2004).
Metals in the sporulation phosphorelay: manganese binding by the response regulator Spo0F.
  Acta Crystallogr D Biol Crystallogr, 60, 638-645.
PDB code: 1pey
15187186 H.Szurmant, and G.W.Ordal (2004).
Diversity in chemotaxis mechanisms among the bacteria and archaea.
  Microbiol Mol Biol Rev, 68, 301-319.  
15491362 R.E.Muir, and J.W.Gober (2004).
Regulation of FlbD activity by flagellum assembly is accomplished through direct interaction with the trans-acting factor, FliX.
  Mol Microbiol, 54, 715-730.  
12486062 C.Birck, Y.Chen, F.M.Hulett, and J.P.Samama (2003).
The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface.
  J Bacteriol, 185, 254-261.
PDB code: 1mvo
12940980 J.A.Hubbard, L.K.MacLachlan, G.W.King, J.J.Jones, and A.P.Fosberry (2003).
Nuclear magnetic resonance spectroscopy reveals the functional state of the signalling protein CheY in vivo in Escherichia coli.
  Mol Microbiol, 49, 1191-1200.  
14563873 J.G.Smith, J.A.Latiolais, G.P.Guanga, S.Citineni, R.E.Silversmith, and R.B.Bourret (2003).
Investigation of the role of electrostatic charge in activation of the Escherichia coli response regulator CheY.
  J Bacteriol, 185, 6385-6391.  
12591865 R.E.Silversmith, G.P.Guanga, L.Betts, C.Chu, R.Zhao, and R.B.Bourret (2003).
CheZ-mediated dephosphorylation of the Escherichia coli chemotaxis response regulator CheY: role for CheY glutamate 89.
  J Bacteriol, 185, 1495-1502.
PDB code: 1mih
12582120 S.W.Porter, Q.Xu, and A.H.West (2003).
Ssk1p response regulator binding surface on histidine-containing phosphotransfer protein Ypd1p.
  Eukaryot Cell, 2, 27-33.  
12455952 A.D.Ault, J.S.Fassler, and R.J.Deschenes (2002).
Altered phosphotransfer in an activated mutant of the Saccharomyces cerevisiae two-component osmosensor Sln1p.
  Eukaryot Cell, 1, 174-180.  
12169605 I.Delany, G.Spohn, R.Rappuoli, and V.Scarlato (2002).
Growth phase-dependent regulation of target gene promoters for binding of the essential orphan response regulator HP1043 of Helicobacter pylori.
  J Bacteriol, 184, 4800-4810.  
12381845 P.Roche, L.Mouawad, D.Perahia, J.P.Samama, and D.Kahn (2002).
Molecular dynamics of the FixJ receiver domain: movement of the beta4-alpha4 loop correlates with the in and out flip of Phe101.
  Protein Sci, 11, 2622-2630.  
12080332 R.Zhao, E.J.Collins, R.B.Bourret, and R.E.Silversmith (2002).
Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ.
  Nat Struct Biol, 9, 570-575.
PDB code: 1kmi
12176983 V.Guillet, N.Ohta, S.Cabantous, A.Newton, and J.P.Samama (2002).
Crystallographic and biochemical studies of DivK reveal novel features of an essential response regulator in Caulobacter crescentus.
  J Biol Chem, 277, 42003-42010.
PDB codes: 1m5t 1m5u 1mav 1mb0 1mb3
11847283 Y.J.Im, S.H.Rho, C.M.Park, S.S.Yang, J.G.Kang, J.Y.Lee, P.S.Song, and S.H.Eom (2002).
Crystal structure of a cyanobacterial phytochrome response regulator.
  Protein Sci, 11, 614-624.
PDB codes: 1i3c 1jlk
11406410 A.H.West, and A.M.Stock (2001).
Histidine kinases and response regulator proteins in two-component signaling systems.
  Trends Biochem Sci, 26, 369-376.  
11528000 C.C.Häse, N.D.Fedorova, M.Y.Galperin, and P.A.Dibrov (2001).
Sodium ion cycle in bacterial pathogens: evidence from cross-genome comparisons.
  Microbiol Mol Biol Rev, 65, 353.  
11169116 E.Hager, H.Tse, and R.E.Gill (2001).
Identification and characterization of spdR mutations that bypass the BsgA protease-dependent regulation of developmental gene expression in Myxococcus xanthus.
  Mol Microbiol, 39, 765-780.  
11244058 M.P.Allen, K.B.Zumbrennen, and W.R.McCleary (2001).
Genetic evidence that the alpha5 helix of the receiver domain of PhoB is involved in interdomain interactions.
  J Bacteriol, 183, 2204-2211.  
11369848 P.Garcia, L.Serrano, D.Durand, M.Rico, and M.Bruix (2001).
NMR and SAXS characterization of the denatured state of the chemotactic protein CheY: implications for protein folding initiation.
  Protein Sci, 10, 1100-1112.  
11134926 P.Gouet, N.Chinardet, M.Welch, V.Guillet, S.Cabantous, C.Birck, L.Mourey, and J.P.Samama (2001).
Further insights into the mechanism of function of the response regulator CheY from crystallographic studies of the CheY--CheA(124--257) complex.
  Acta Crystallogr D Biol Crystallogr, 57, 44-51.
PDB codes: 1ffg 1ffs 1ffw
11169108 T.Fuchs, P.Wiget, M.Osterås, and U.Jenal (2001).
Precise amounts of a novel member of a phosphotransferase superfamily are essential for growth and normal morphology in Caulobacter crescentus.
  Mol Microbiol, 39, 679-692.  
10966457 A.M.Stock, V.L.Robinson, and P.N.Goudreau (2000).
Two-component signal transduction.
  Annu Rev Biochem, 69, 183-215.  
10632881 D.S.Shah, S.L.Porter, D.C.Harris, G.H.Wadhams, P.A.Hamblin, and J.P.Armitage (2000).
Identification of a fourth cheY gene in Rhodobacter sphaeroides and interspecies interaction within the bacterial chemotaxis signal transduction pathway.
  Mol Microbiol, 35, 101-112.  
  10850799 G.S.Anand, P.N.Goudreau, J.K.Lewis, and A.M.Stoc (2000).
Evidence for phosphorylation-dependent conformational changes in methylesterase CheB.
  Protein Sci, 9, 898-906.  
10894737 H.Li, and L.A.Sherman (2000).
A redox-responsive regulator of photosynthesis gene expression in the cyanobacterium Synechocystis sp. Strain PCC 6803.
  J Bacteriol, 182, 4268-4277.  
10924144 J.A.Bornhorst, and J.J.Falke (2000).
Attractant regulation of the aspartate receptor-kinase complex: limited cooperative interactions between receptors and effects of the receptor modification state.
  Biochemistry, 39, 9486-9493.  
10613863 J.K.Cheung, and J.I.Rood (2000).
The VirR response regulator from Clostridium perfringens binds independently to two imperfect direct repeats located upstream of the pfoA promoter.
  J Bacteriol, 182, 57-66.  
10837243 J.Stock, and S.Da Re (2000).
Signal transduction: response regulators on and off.
  Curr Biol, 10, R420-R424.  
11052668 R.C.Stewart, K.Jahreis, and J.S.Parkinson (2000).
Rapid phosphotransfer to CheY from a CheA protein lacking the CheY-binding domain.
  Biochemistry, 39, 13157-13165.  
11094272 V.Rangaswamy, and C.L.Bender (2000).
Phosphorylation of CorS and CorR, regulatory proteins that modulate production of the phytotoxin coronatine in Pseudomonas syringae.
  FEMS Microbiol Lett, 193, 13-18.  
10647181 C.Birck, L.Mourey, P.Gouet, B.Fabry, J.Schumacher, P.Rousseau, D.Kahn, and J.P.Samama (1999).
Conformational changes induced by phosphorylation of the FixJ receiver domain.
  Structure, 7, 1505-1515.
PDB code: 1d5w
10647185 H.J.Müller-Dieckmann, A.A.Grantz, and S.H.Kim (1999).
The structure of the signal receiver domain of the Arabidopsis thaliana ethylene receptor ETR1.
  Structure, 7, 1547-1556.
PDB code: 1dcf
10491176 H.Schüler, E.Korenbaum, C.E.Schutt, U.Lindberg, and R.Karlsson (1999).
Mutational analysis of Ser14 and Asp157 in the nucleotide-binding site of beta-actin.
  Eur J Biochem, 265, 210-220.  
  10419963 I.Rombel, P.Peters-Wendisch, A.Mesecar, T.Thorgeirsson, Y.K.Shin, and S.Kustu (1999).
MgATP binding and hydrolysis determinants of NtrC, a bacterial enhancer-binding protein.
  J Bacteriol, 181, 4628-4638.  
  10390224 J.J.Hilliard, R.M.Goldschmidt, L.Licata, E.Z.Baum, and K.Bush (1999).
Multiple mechanisms of action for inhibitors of histidine protein kinases from bacterial two-component systems.
  Antimicrob Agents Chemother, 43, 1693-1699.  
10594818 J.L.Appleby, and R.B.Bourret (1999).
Activation of CheY mutant D57N by phosphorylation at an alternative site, Ser-56.
  Mol Microbiol, 34, 915-925.  
10545127 M.D.Nichols, K.DeAngelis, J.L.Keck, and J.M.Berger (1999).
Structure and function of an archaeal topoisomerase VI subunit with homology to the meiotic recombination factor Spo11.
  EMBO J, 18, 6177-6188.
PDB code: 1d3y
10393292 M.Kato, T.Shimizu, T.Mizuno, and T.Hakoshima (1999).
Structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor protein ArcB complexed with the chemotaxis response regulator CheY.
  Acta Crystallogr D Biol Crystallogr, 55, 1257-1263.
PDB code: 1bdj
10647182 P.Gouet, B.Fabry, V.Guillet, C.Birck, L.Mourey, D.Kahn, and J.P.Samama (1999).
Structural transitions in the FixJ receiver domain.
  Structure, 7, 1517-1526.
PDB codes: 1dbw 1dck 1dcm
10029518 T.L.Mayover, C.J.Halkides, and R.C.Stewart (1999).
Kinetic characterization of CheY phosphorylation reactions: comparison of P-CheA and small-molecule phosphodonors.
  Biochemistry, 38, 2259-2271.  
9753454 C.J.Halkides, X.Zhu, D.P.Phillion, P.Matsumura, and F.W.Dahlquist (1998).
Synthesis and biochemical characterization of an analogue of CheY-phosphate, a signal transduction protein in bacterial chemotaxis.
  Biochemistry, 37, 13674-13680.  
  9657998 J.L.Appleby, and R.B.Bourret (1998).
Proposed signal transduction role for conserved CheY residue Thr87, a member of the response regulator active-site quintet.
  J Bacteriol, 180, 3563-3569.  
9653108 J.M.Berger, D.Fass, J.C.Wang, and S.C.Harrison (1998).
Structural similarities between topoisomerases that cleave one or both DNA strands.
  Proc Natl Acad Sci U S A, 95, 7876-7881.  
9636149 M.M.McEvoy, A.C.Hausrath, G.B.Randolph, S.J.Remington, and F.W.Dahlquist (1998).
Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway.
  Proc Natl Acad Sci U S A, 95, 7333-7338.
PDB code: 1eay
9687374 M.S.Jurica, and B.L.Stoddard (1998).
Mind your B's and R's: bacterial chemotaxis, signal transduction and protein recognition.
  Structure, 6, 809-813.  
10089524 M.Staley, L.C.Zeringue, R.D.Kidd, B.T.Nixon, and G.K.Farber (1998).
Crystallization and preliminary X-ray studies of the Rhizobium meliloti DctD two-component receiver domain.
  Acta Crystallogr D Biol Crystallogr, 54, 1416-1418.  
9437425 M.Welch, N.Chinardet, L.Mourey, C.Birck, and J.P.Samama (1998).
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY.
  Nat Struct Biol, 5, 25-29.
PDB code: 1a0o
10066483 P.N.Goudreau, and A.M.Stock (1998).
Signal transduction in bacteria: molecular mechanisms of stimulus-response coupling.
  Curr Opin Microbiol, 1, 160-169.  
9465023 S.Djordjevic, P.N.Goudreau, Q.Xu, A.M.Stock, and A.H.West (1998).
Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain.
  Proc Natl Acad Sci U S A, 95, 1381-1386.
PDB code: 1a2o
9540996 V.A.Feher, Y.L.Tzeng, J.A.Hoch, and J.Cavanagh (1998).
Identification of communication networks in Spo0F: a model for phosphorylation-induced conformational change and implications for activation of multiple domain bacterial response regulators.
  FEBS Lett, 425, 1-6.  
9442881 J.J.Falke, R.B.Bass, S.L.Butler, S.A.Chervitz, and M.A.Danielson (1997).
The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymes.
  Annu Rev Cell Dev Biol, 13, 457-512.  
8999880 J.L.Dahl, B.Y.Wei, and R.J.Kadner (1997).
Protein phosphorylation affects binding of the Escherichia coli transcription activator UhpA to the uhpT promoter.
  J Biol Chem, 272, 1910-1919.  
9054511 M.Kato, T.Mizuno, T.Shimizu, and T.Hakoshima (1997).
Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB.
  Cell, 88, 717-723.
PDB code: 1a0b
9335530 M.Madhusudan, J.Zapf, J.A.Hoch, J.M.Whiteley, N.H.Xuong, and K.I.Varughese (1997).
A response regulatory protein with the site of phosphorylation blocked by an arginine interaction: crystal structure of Spo0F from Bacillus subtilis.
  Biochemistry, 36, 12739-12745.
PDB code: 1nat
9218420 S.Ma, D.J.Wozniak, and D.E.Ohman (1997).
Identification of the histidine protein kinase KinB in Pseudomonas aeruginosa and its phosphorylation of the alginate regulator algB.
  J Biol Chem, 272, 17952-17960.  
9254596 V.A.Feher, J.W.Zapf, J.A.Hoch, J.M.Whiteley, L.P.McIntosh, M.Rance, N.J.Skelton, F.W.Dahlquist, and J.Cavanagh (1997).
High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: implications for phosphorylation and molecular recognition.
  Biochemistry, 36, 10015-10025.
PDB codes: 1fsp 2fsp
  9171423 W.Hsing, and T.J.Silhavy (1997).
Function of conserved histidine-243 in phosphatase activity of EnvZ, the sensor for porin osmoregulation in Escherichia coli.
  J Bacteriol, 179, 3729-3735.  
  8755904 C.H.Chang, J.Zhu, and S.C.Winans (1996).
Pleiotropic phenotypes caused by genetic ablation of the receiver module of the Agrobacterium tumefaciens VirA protein.
  J Bacteriol, 178, 4710-4716.  
8780507 I.Baikalov, I.Schröder, M.Kaczor-Grzeskowiak, K.Grzeskowiak, R.P.Gunsalus, and R.E.Dickerson (1996).
Structure of the Escherichia coli response regulator NarL.
  Biochemistry, 35, 11053-11061.
PDB code: 1rnl
8703943 K.Scheffzek, W.Kliche, L.Wiesmüller, and J.Reinstein (1996).
Crystal structure of the complex of UMP/CMP kinase from Dictyostelium discoideum and the bisubstrate inhibitor P1-(5'-adenosyl) P5-(5'-uridyl) pentaphosphate (UP5A) and Mg2+ at 2.2 A: implications for water-mediated specificity.
  Biochemistry, 35, 9716-9727.
PDB codes: 1ukd 1uke
8800468 M.A.Danielson, and J.J.Falke (1996).
Use of 19F NMR to probe protein structure and conformational changes.
  Annu Rev Biophys Biomol Struct, 25, 163-195.  
8805550 Madhusudan, J.Zapf, J.M.Whiteley, J.A.Hoch, N.H.Xuong, and K.I.Varughese (1996).
Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis.
  Structure, 4, 679-690.
PDB code: 1srr
  8550470 R.V.Swanson, M.G.Sanna, and M.I.Simon (1996).
Thermostable chemotaxis proteins from the hyperthermophilic bacterium Thermotoga maritima.
  J Bacteriol, 178, 484-489.  
  8763950 X.Zhu, C.D.Amsler, K.Volz, and P.Matsumura (1996).
Tyrosine 106 of CheY plays an important role in chemotaxis signal transduction in Escherichia coli.
  J Bacteriol, 178, 4208-4215.  
8749361 A.M.Stock, and S.L.Mowbray (1995).
Bacterial chemotaxis: a field in motion.
  Curr Opin Struct Biol, 5, 744-751.  
7596290 C.A.Webber, and R.J.Kadner (1995).
Action of receiver and activator modules of UhpA in transcriptional control of the Escherichia coli sugar phosphate transport system.
  Mol Microbiol, 15, 883-893.  
  7603411 K.E.Sanderson, A.Hessel, and K.E.Rudd (1995).
Genetic map of Salmonella typhimurium, edition VIII.
  Microbiol Rev, 59, 241-303.  
7552716 R.V.Swanson, D.F.Lowry, P.Matsumura, M.M.McEvoy, M.I.Simon, and F.W.Dahlquist (1995).
Localized perturbations in CheY structure monitored by NMR identify a CheA binding interface.
  Nat Struct Biol, 2, 906-910.  
7615544 S.Ganguli, H.Wang, P.Matsumura, and K.Volz (1995).
Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.1-A structure of a threonine to isoleucine mutant at position 87 of CheY.
  J Biol Chem, 270, 17386-17393.
PDB code: 1vlz
  8528078 V.A.Feher, J.W.Zapf, J.A.Hoch, F.W.Dahlquist, J.M.Whiteley, and J.Cavanagh (1995).
1H, 15N, and 13C backbone chemical shift assignments, secondary structure, and magnesium-binding characteristics of the Bacillus subtilis response regulator, Spo0F, determined by heteronuclear high-resolution NMR.
  Protein Sci, 4, 1801-1814.  
7899550 J.J.Falke, S.K.Drake, A.L.Hazard, and O.B.Peersen (1994).
Molecular tuning of ion binding to calcium signaling proteins.
  Q Rev Biophys, 27, 219-290.  
7812134 J.Stock, M.Surette, and P.Park (1994).
Chemosensing and signal transduction in bacteria.
  Curr Opin Neurobiol, 4, 474-480.  
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