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protein metals Protein-protein interface(s) links
Chemotaxis PDB id
1a0o
Jmol
Contents
Protein chains
128 a.a. *
70 a.a. *
Metals
_MN ×4
* Residue conservation analysis
PDB id:
1a0o
Name: Chemotaxis
Title: Chey-binding domain of chea in complex with chey
Structure: Chey. Chain: a, c, e, g. Engineered: yes. Chea. Chain: b, d, f, h. Fragment: chea 124-257. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Cellular_location: cytoplasm. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
2.95Å     R-factor:   0.187     R-free:   0.235
Authors: N.Chinardet,M.Welch,L.Mourey,C.Birck,J.P.Samama
Key ref: M.Welch et al. (1998). Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY. Nat Struct Biol, 5, 25-29. PubMed id: 9437425 DOI: 10.1038/nsb0198-25
Date:
05-Dec-97     Release date:   30-Dec-98    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0AE67  (CHEY_ECOLI) -  Chemotaxis protein CheY
Seq:
Struc: 		129 a.a.
128 a.a.
Protein chains
Pfam   ArchSchema ?
P07363  (CHEA_ECOLI) -  Chemotaxis protein CheA
Seq:
Struc: 		 
Seq:
Struc: 		654 a.a.
70 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains B, D, F, H: E.C.2.7.13.3  - Histidine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
ATP
 + protein L-histidine
 = ADP
 + protein N-phospho-L-histidine
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     intracellular signal transduction   7 terms 
  Biochemical function     two-component response regulator activity     3 terms  

 

 
    reference    
 
 
DOI no: 10.1038/nsb0198-25 Nat Struct Biol 5:25-29 (1998)
PubMed id: 9437425  
 
 
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY.
M.Welch, N.Chinardet, L.Mourey, C.Birck, J.P.Samama.
 
  ABSTRACT  
 
Bacterial adaptation to the environment is accomplished through the coordinated activation of specific sensory receptors and signal processing proteins. Among the best characterized of these pathways are those which employ the two-component paradigm. In these systems, signal transmission is mediated by Mg(2+)-dependent phospho-relay reactions between histidine auto-kinases and phospho-accepting receiver domains in response-regulator proteins. Although this mechanism of activation is common to all response-regulators, detrimental cross-talk between different two-component pathways within the same cell is minimized through the use of specific recognition domains. Here, we report the crystal structure, at 2.95 A resolution, of the response regulator of bacterial chemotaxis, CheY, bound to the recognition domain from its cognate histidine kinase, CheA. The structure suggests that molecular recognition, in this low affinity complex (KD = 2 microM), may also contribute to the mechanism of CheY activation.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20355710 J.Bhatnagar, P.P.Borbat, A.M.Pollard, A.M.Bilwes, J.H.Freed, and B.R.Crane (2010).
Structure of the ternary complex formed by a chemotaxis receptor signaling domain, the CheA histidine kinase, and the coupling protein CheW as determined by pulsed dipolar ESR spectroscopy.
  Biochemistry, 49, 3824-3841.  
19505148 A.K.Eaton, and R.C.Stewart (2009).
The two active sites of Thermotoga maritima CheA dimers bind ATP with dramatically different affinities.
  Biochemistry, 48, 6412-6422.  
19836334 S.Yamada, H.Sugimoto, M.Kobayashi, A.Ohno, H.Nakamura, and Y.Shiro (2009).
Structure of PAS-linked histidine kinase and the response regulator complex.
  Structure, 17, 1333-1344.
PDB codes: 3a0r 3a0s 3a0t 3a0u 3a0v 3a0w 3a0x 3a0y 3a0z 3a10
18076326 M.T.Laub, and M.Goulian (2007).
Specificity in two-component signal transduction pathways.
  Annu Rev Genet, 41, 121-145.  
16815921 K.N.Rao, D.Kumaran, J.Seetharaman, J.B.Bonanno, S.K.Burley, and S.Swaminathan (2006).
Crystal structure of trehalose-6-phosphate phosphatase-related protein: biochemical and biological implications.
  Protein Sci, 15, 1735-1744.
PDB code: 1u02
16369945 M.D.Baker, P.M.Wolanin, and J.B.Stock (2006).
Signal transduction in bacterial chemotaxis.
  Bioessays, 28, 9.  
16973743 P.M.Wolanin, M.D.Baker, N.R.Francis, D.R.Thomas, D.J.DeRosier, and J.B.Stock (2006).
Self-assembly of receptor/signaling complexes in bacterial chemotaxis.
  Proc Natl Acad Sci U S A, 103, 14313-14318.  
15778956 D.Segal, and M.Eisenstein (2005).
The effect of resolution-dependent global shape modifications on rigid-body protein-protein docking.
  Proteins, 59, 580-591.  
  16511085 H.Wang, H.Pang, Y.Ding, Y.Li, X.Wu, and Z.Rao (2005).
Purification, crystallization and preliminary X-ray diffraction analysis of human enolase-phosphatase E1.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 521-523.  
16321923 K.I.Varughese (2005).
Conformational changes of Spo0F along the phosphotransfer pathway.
  J Bacteriol, 187, 8221-8227.  
15987886 M.Jäger, X.Michalet, and S.Weiss (2005).
Protein-protein interactions as a tool for site-specific labeling of proteins.
  Protein Sci, 14, 2059-2068.  
15162493 A.Berchanski, B.Shapira, and M.Eisenstein (2004).
Hydrophobic complementarity in protein-protein docking.
  Proteins, 56, 130-142.  
15240481 C.Benda, C.Scheufler, N.Tandeau de Marsac, and W.Gärtner (2004).
Crystal structures of two cyanobacterial response regulators in apo- and phosphorylated form reveal a novel dimerization motif of phytochrome-associated response regulators.
  Biophys J, 87, 476-487.
PDB codes: 1k66 1k68
15090529 C.J.Bent, N.W.Isaacs, T.J.Mitchell, and A.Riboldi-Tunnicliffe (2004).
Crystal structure of the response regulator 02 receiver domain, the essential YycF two-component system of Streptococcus pneumoniae in both complexed and native states.
  J Bacteriol, 186, 2872-2879.
PDB codes: 1nxo 1nxp 1nxt 1nxw
15573139 G.H.Wadhams, and J.P.Armitage (2004).
Making sense of it all: bacterial chemotaxis.
  Nat Rev Mol Cell Biol, 5, 1024-1037.  
15572451 N.R.Francis, P.M.Wolanin, J.B.Stock, D.J.Derosier, and D.R.Thomas (2004).
Three-dimensional structure and organization of a receptor/signaling complex.
  Proc Natl Acad Sci U S A, 101, 17480-17485.  
15289606 S.Y.Park, B.D.Beel, M.I.Simon, A.M.Bilwes, and B.R.Crane (2004).
In different organisms, the mode of interaction between two signaling proteins is not necessarily conserved.
  Proc Natl Acad Sci U S A, 101, 11646-11651.
PDB code: 1u0s
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
12824492 D.H.Shin, A.Roberts, J.Jancarik, H.Yokota, R.Kim, D.E.Wemmer, and S.H.Kim (2003).
Crystal structure of a phosphatase with a unique substrate binding domain from Thermotoga maritima.
  Protein Sci, 12, 1464-1472.
PDB code: 1nf2
12511501 G.Alexandre, and I.B.Zhulin (2003).
Different evolutionary constraints on chemotaxis proteins CheW and CheY revealed by heterologous expression studies and protein sequence analysis.
  J Bacteriol, 185, 544-552.  
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.  
12718534 S.J.Landry (2003).
Structure and energetics of an allele-specific genetic interaction between dnaJ and dnaK: correlation of nuclear magnetic resonance chemical shift perturbations in the J-domain of Hsp40/DnaJ with binding affinity for the ATPase domain of Hsp70/DnaK.
  Biochemistry, 42, 4926-4936.  
12406212 D.Fink, N.Weissschuh, J.Reuther, W.Wohlleben, and A.Engels (2002).
Two transcriptional regulators GlnR and GlnRII are involved in regulation of nitrogen metabolism in Streptomyces coelicolor A3(2).
  Mol Microbiol, 46, 331-347.  
12022879 G.S.Anand, and A.M.Stock (2002).
Kinetic basis for the stimulatory effect of phosphorylation on the methylesterase activity of CheB.
  Biochemistry, 41, 6752-6760.  
12119289 M.N.Levit, T.W.Grebe, and J.B.Stock (2002).
Organization of the receptor-kinase signaling array that regulates Escherichia coli chemotaxis.
  J Biol Chem, 277, 36748-36754.  
12119290 N.R.Francis, M.N.Levit, T.R.Shaikh, L.A.Melanson, J.B.Stock, and D.J.DeRosier (2002).
Subunit organization in a soluble complex of tar, CheW, and CheA by electron microscopy.
  J Biol Chem, 277, 36755-36759.  
12438647 S.B.Williams, I.Vakonakis, S.S.Golden, and A.C.LiWang (2002).
Structure and function from the circadian clock protein KaiA of Synechococcus elongatus: a potential clock input mechanism.
  Proc Natl Acad Sci U S A, 99, 15357-15362.
PDB codes: 1m2e 1m2f
12381847 S.Da Re, T.Tolstykh, P.M.Wolanin, and J.B.Stock (2002).
Genetic analysis of response regulator activation in bacterial chemotaxis suggests an intermolecular mechanism.
  Protein Sci, 11, 2644-2654.  
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.  
11353835 M.Schuster, R.E.Silversmith, and R.B.Bourret (2001).
Conformational coupling in the chemotaxis response regulator CheY.
  Proc Natl Acad Sci U S A, 98, 6003-6008.  
11422367 T.Hübschmann, H.J.Jorissen, T.Börner, W.Gärtner, and N.Tandeau de Marsac (2001).
Phosphorylation of proteins in the light-dependent signalling pathway of a filamentous cyanobacterium.
  Eur J Biochem, 268, 3383-3389.  
11092844 A.Bren, and M.Eisenbach (2000).
How signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation.
  J Bacteriol, 182, 6865-6873.  
10966457 A.M.Stock, V.L.Robinson, and P.N.Goudreau (2000).
Two-component signal transduction.
  Annu Rev Biochem, 69, 183-215.  
11019801 A.N.Stepanova, and J.R.Ecker (2000).
Ethylene signaling: from mutants to molecules.
  Curr Opin Plant Biol, 3, 353-360.  
10660286 J.Stock, and M.Levit (2000).
Signal transduction: hair brains in bacterial chemotaxis.
  Curr Biol, 10, R11-R14.  
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.  
  10203840 A.L.Perraud, V.Weiss, and R.Gross (1999).
Signalling pathways in two-component phosphorelay systems.
  Trends Microbiol, 7, 115-120.  
9989504 A.M.Bilwes, L.A.Alex, B.R.Crane, and M.I.Simon (1999).
Structure of CheA, a signal-transducing histidine kinase.
  Cell, 96, 131-141.
PDB code: 1b3q
9867810 A.Richardson, S.M.van der Vies, F.Keppel, A.Taher, S.J.Landry, and C.Georgopoulos (1999).
Compensatory changes in GroEL/Gp31 affinity as a mechanism for allele-specific genetic interaction.
  J Biol Chem, 274, 52-58.  
  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
  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.  
10339418 J.Stock (1999).
Signal transduction: Gyrating protein kinases.
  Curr Biol, 9, R364-R367.  
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.  
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 codes are shown on the right.