PDBsum entry 1cye

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protein links
Signal transduction PDB id
Protein chain
129 a.a. *
* Residue conservation analysis
PDB id:
Name: Signal transduction
Title: Three dimensional structure of chemotactic che y protein in aqueous solution by nuclear magnetic resonance methods
Structure: Chey. Chain: a. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562.
NMR struc: 20 models
Authors: J.Santoro,M.Bruix,J.Pascual,E.Lopez,L.Serrano,M.Rico
Key ref: J.Santoro et al. (1995). Three-dimensional structure of chemotactic Che Y protein in aqueous solution by nuclear magnetic resonance methods. J Mol Biol, 247, 717-725. PubMed id: 7723026
21-Oct-94     Release date:   07-Feb-95    
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Protein chain
Pfam   ArchSchema ?
P0AE67  (CHEY_ECOLI) -  Chemotaxis protein CheY
129 a.a.
129 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     intracellular signal transduction   7 terms 
  Biochemical function     protein binding     5 terms  


J Mol Biol 247:717-725 (1995)
PubMed id: 7723026  
Three-dimensional structure of chemotactic Che Y protein in aqueous solution by nuclear magnetic resonance methods.
J.Santoro, M.Bruix, J.Pascual, E.López, L.Serrano, M.Rico.
The three-dimensional structure of chemotactic Che Y protein from Escherichia coli in aqueous solution has been determined by nuclear magnetic resonance (NMR) spectroscopy combined with restrained molecular dynamics calculations. A total of 20 converged structures were computed from 1545 conformationally relevant distance restraints derived from 1858 unambiguously assigned NOE cross-correlations. The resulting average pairwise root-mean-square deviation is 1.03 A for the backbone atoms and 1.69 A for all heavy atoms. If residues in the regions structurally least defined (1 to 5, 47 to 50, 76 to 79, 88 to 91 and 124 to 129) are excluded from the analysis, the root-mean-square deviations are reduced to 0.53 A and 1.23 A, respectively. The solution structure is closely similar to the refined X-ray crystal structure, except in the regions found to be less defined by NMR spectroscopy. The root-mean-square deviation between the average solution structure and the X-ray crystal structure is 0.92 A for the backbone residues (2 to 129). The highly refined solution structure determined herewith provides an essential background to delineate functionally important conformational changes brought about by different effectors.

Literature references that cite this PDB file's key reference

  PubMed id Reference
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.  
12220489 P.Garcia, L.Serrano, M.Rico, and M.Bruix (2002).
An NMR view of the folding process of a CheY mutant at the residue level.
  Structure, 10, 1173-1185.  
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.  
10966457 A.M.Stock, V.L.Robinson, and P.N.Goudreau (2000).
Two-component signal transduction.
  Annu Rev Biochem, 69, 183-215.  
10611291 D.Yan, H.S.Cho, C.A.Hastings, M.M.Igo, S.Y.Lee, J.G.Pelton, V.Stewart, D.E.Wemmer, and S.Kustu (1999).
Beryllofluoride mimics phosphorylation of NtrC and other bacterial response regulators.
  Proc Natl Acad Sci U S A, 96, 14789-14794.  
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.  
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
  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.  
9560203 R.Ramakrishnan, M.Schuster, and R.B.Bourret (1998).
Acetylation at Lys-92 enhances signaling by the chemotaxis response regulator protein CheY.
  Proc Natl Acad Sci U S A, 95, 4918-4923.  
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.  
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
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
  8520484 V.Muñoz, F.J.Blanco, and L.Serrano (1995).
The distribution of alpha-helix propensity along the polypeptide chain is not conserved in proteins from the same family.
  Protein Sci, 4, 1577-1586.  
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.