PDBsum entry 1ymv

Go to PDB code: 
protein metals links
Chemotaxis PDB id
Protein chain
124 a.a. *
Waters ×87
* Residue conservation analysis
PDB id:
Name: Chemotaxis
Title: Signal transduction protein chey mutant with phe 14 replaced by gly, ser 15 replaced by gly, and met 17 replaced by gly
Structure: Chey. Chain: a. Engineered: yes. Mutation: yes. Other_details: mg2+ bound in the active site
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562. (Pharmacia)
1.90Å     R-factor:   0.187    
Authors: L.Bellsolell,M.Coll
Key ref:
L.Bellsolell et al. (1996). The three-dimensional structure of two mutants of the signal transduction protein CheY suggest its molecular activation mechanism. J Mol Biol, 257, 116-128. PubMed id: 8632450 DOI: 10.1006/jmbi.1996.0151
14-Dec-95     Release date:   03-Apr-96    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P0AE67  (CHEY_ECOLI) -  Chemotaxis protein CheY
129 a.a.
124 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     bacterial-type flagellar cell motility   6 terms 
  Biochemical function     protein binding     4 terms  


DOI no: 10.1006/jmbi.1996.0151 J Mol Biol 257:116-128 (1996)
PubMed id: 8632450  
The three-dimensional structure of two mutants of the signal transduction protein CheY suggest its molecular activation mechanism.
L.Bellsolell, P.Cronet, M.Majolero, L.Serrano, M.Coll.
The three-dimensional crystal structures of the single mutant M17G and the triple mutant F14G-S15G-M17G of the response regulator protein CheY have been determined to 2.3 and 1.9 angstrom, respectively. Both mutants bind the essential Mg2+ cation as determined by the changes in stability, but binding does not cause the intrinsic fluorescence quenching of W58 observed in the wild-type protein. The loop beta4-alpha4 appears to be very flexible in both mutants and helix alpha4, which starts at N94 in the native Mg2+-CheY and at K91 in the native apo-CheY, starts in both mutants at residue K92. The side-chain of K109 appears to be more mobile because of the space freed by the M17G mutation. In the triple mutant the main chain of K109 and adjacent residues (loop beta5-alpha5) is displaced almost by 2 angstrom affecting the main chain at residues T87 to E89 (C terminus of beta4). The triple mutant structure has a Mg2+ bound at the active site, but although the Mg2+ coordination is similar to that of the native Mg2+-CheY, the structural consequences of the metal binding are quite different. It seems that the mutations have disrupted the mechanism of movement transmission observed in the native protein. We suggest that the side-chain of K109, packed between V86, A88 and M17 in the native protein, slides forwards and backwards upon activation and deactivation dragging the main chain at the loop beta5-alpha5 and triggering larger movements at the functional surface of the protein.
  Selected figure(s)  
Figure 1.
Figure 1. Ball and stick diagram showing the N terminus of helix a4 and the preceding loop in CheY-M1. The helix starts with a 310 turn at Lys92. Key residues for the packing of the helix against the protein core like Tyr106, Thr87, Trp58, Asn94 and Ile95 are shown.
Figure 8.
Figure 8. Superimposition of Mg 2+ -CheY-M2 (white; this work), apo-CheY (green; Volz & Matsumura, 1991) and Mg 2+ -CheY (blue; Bellsolell et al., 1994) at the active pocket. The side-chain of Lys109 is disordered in the Mg 2+ -CheY-M2 structure. The sites of the three mutations, Phe14Gly, Ser15Gly and Met17Gly, in Mg 2+ -CheY-M2 are shown. Some side-chains were removed for clarity.
  The above figures are reprinted by permission from Elsevier: J Mol Biol (1996, 257, 116-128) copyright 1996.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
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
19714199 B.A.Kidd, D.Baker, and W.E.Thomas (2009).
Computation of conformational coupling in allosteric proteins.
  PLoS Comput Biol, 5, e1000484.  
16929106 M.Solà, D.L.Drew, A.G.Blanco, F.X.Gomis-Rüth, and M.Coll (2006).
The cofactor-induced pre-active conformation in PhoB.
  Acta Crystallogr D Biol Crystallogr, 62, 1046-1057.
PDB code: 2iyn
10966457 A.M.Stock, V.L.Robinson, and P.N.Goudreau (2000).
Two-component signal transduction.
  Annu Rev Biochem, 69, 183-215.  
9727015 D.Shukla, X.Y.Zhu, and P.Matsumura (1998).
Flagellar motor-switch binding face of CheY and the biochemical basis of suppression by CheY mutants that compensate for motor-switch defects in Escherichia coli.
  J Biol Chem, 273, 23993-23999.  
9761905 D.Wilcock, M.T.Pisabarro, E.López-Hernandez, L.Serrano, and M.Coll (1998).
Structure analysis of two CheY mutants: importance of the hydrogen-bond contribution to protein stability.
  Acta Crystallogr D Biol Crystallogr, 54, 378-385.
PDB codes: 1ab5 1ab6
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.  
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.  
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.  
9030763 M.Bruix, V.Muñoz, R.Campos-Olivas, J.R.Del Bosque, L.Serrano, and M.Rico (1997).
Characterisation of the isolated Che Y C-terminal fragment (79-129)--Exploring the structure/stability/folding relationship of the alpha/beta parallel protein Che Y.
  Eur J Biochem, 243, 384-392.  
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
8962056 A.Haldimann, M.K.Prahalad, S.L.Fisher, S.K.Kim, C.T.Walsh, and B.L.Wanner (1996).
Altered recognition mutants of the response regulator PhoB: a new genetic strategy for studying protein-protein interactions.
  Proc Natl Acad Sci U S A, 93, 14361-14366.  
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.