spacer
spacer

PDBsum entry 1cey

Go to PDB code: 
protein links
Signal transduction PDB id
1cey
Jmol
Contents
Protein chain
128 a.a. *
* Residue conservation analysis
PDB id:
1cey
Name: Signal transduction
Title: Assignments, secondary structure, global fold, and dynamics of chemotaxis y protein using three-and four-dimensional heteronuclear (13c,15n) nmr spectroscopy
Structure: Chey. Chain: a. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562.
NMR struc: 46 models
Authors: F.J.Moy,D.F.Lowry,P.Matsumura,F.W.Dahlquist,J.E.Krywko, P.J.Domaille
Key ref:
F.J.Moy et al. (1994). Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy. Biochemistry, 33, 10731-10742. PubMed id: 8075074 DOI: 10.1021/bi00201a022
Date:
23-Nov-94     Release date:   07-Feb-95    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0AE67  (CHEY_ECOLI) -  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   7 terms 
  Biochemical function     protein binding     5 terms  

 

 
DOI no: 10.1021/bi00201a022 Biochemistry 33:10731-10742 (1994)
PubMed id: 8075074  
 
 
Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy.
F.J.Moy, D.F.Lowry, P.Matsumura, F.W.Dahlquist, J.E.Krywko, P.J.Domaille.
 
  ABSTRACT  
 
NMR spectroscopy has been used to study recombinant Escherichia coli CheY, a 128-residue protein involved in regulating bacterial chemotaxis. Heteronuclear three- and four-dimensional (3D and 4D) experiments have provided sequence-specific resonance assignments and quantitation of short-, medium-, and long-range distance restraints from nuclear Overhauser enhancement (NOE) intensities. These distance restraints were further supplemented with measurements of three-bond scalar coupling constants to define the local dihedral angles, and with the identification of amide protons undergoing slow solvent exchange from which hydrogen-bonding patterns were identified. The current model structure shows the same global fold of CheY as existing X-ray structures (Volz & Matsumura, 1991; Stock et al. 1993) with a (beta/alpha)5 motif of five parallel beta-strands at the central core surrounded by three alpha-helices on one face and with two on the opposite side. Heteronuclear 15N-1H relaxation experiments are interpreted to show portions of the protein structure in the Mg2+ binding loop are ill-defined because of slow motion (chemical exchange) on the NMR time scale. Moreover, the presence of Mg2+ disrupts the salt bridge between the highly conserved Lys-109 and Asp-57, the site of phosphorylation.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21456702 K.Itoh, and M.Sasai (2011).
Statistical mechanics of protein allostery: roles of backbone and side-chain structural fluctuations.
  J Chem Phys, 134, 125102.  
20385843 K.Itoh, and M.Sasai (2010).
Entropic mechanism of large fluctuation in allosteric transition.
  Proc Natl Acad Sci U S A, 107, 7775-7780.  
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.  
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
15772084 M.A.Seeliger, M.Spichty, S.E.Kelly, M.Bycroft, S.M.Freund, M.Karplus, and L.S.Itzhaki (2005).
Role of conformational heterogeneity in domain swapping and adapter function of the Cks proteins.
  J Biol Chem, 280, 30448-30459.  
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
14731287 J.G.Smith, J.A.Latiolais, G.P.Guanga, J.D.Pennington, R.E.Silversmith, and R.B.Bourret (2004).
A search for amino acid substitutions that universally activate response regulators.
  Mol Microbiol, 51, 887-901.  
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.  
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
11790828 B.Ma, M.Shatsky, H.J.Wolfson, and R.Nussinov (2002).
Multiple diverse ligands binding at a single protein site: a matter of pre-existing populations.
  Protein Sci, 11, 184-197.  
12202384 S.Kumar, and R.Nussinov (2002).
Relationship between ion pair geometries and electrostatic strengths in proteins.
  Biophys J, 83, 1595-1612.  
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
11264542 B.F.Volkman, D.Lipson, D.E.Wemmer, and D.Kern (2001).
Two-state allosteric behavior in a single-domain signaling protein.
  Science, 291, 2429-2433.  
11269305 M.Buck, and M.K.Rosen (2001).
Structural biology. Flipping a switch.
  Science, 291, 2329-2330.  
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.  
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.  
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.  
  9521117 K.C.Usher, A.F.de la Cruz, F.W.Dahlquist, R.V.Swanson, M.I.Simon, and S.J.Remington (1998).
Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability.
  Protein Sci, 7, 403-412.
PDB codes: 1tmy 2tmy 3tmy 4tmy
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
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
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.  
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
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
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.  
8749361 A.M.Stock, and S.L.Mowbray (1995).
Bacterial chemotaxis: a field in motion.
  Curr Opin Struct Biol, 5, 744-751.  
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.  
  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.  
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.