PDBsum entry 3tmy

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protein metals Protein-protein interface(s) links
Chemotaxis PDB id
Protein chains
118 a.a. *
_MN ×2
Waters ×38
* Residue conservation analysis
PDB id:
Name: Chemotaxis
Title: Chey from thermotoga maritima (mn-iii)
Structure: Chey protein. Chain: a, b. Synonym: tmy. Engineered: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Cellular_location: cytoplasm. Gene: chey. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.20Å     R-factor:   0.182    
Authors: K.C.Usher,A.De La Cruz,F.W.Dahlquist,S.J.Remington
Key ref: K.C.Usher et al. (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. PubMed id: 9521117 DOI: 10.1002/pro.5560070221
04-Jun-97     Release date:   03-Dec-97    
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Protein chains
Pfam   ArchSchema ?
Q56312  (CHEY_THEMA) -  Chemotaxis protein CheY
120 a.a.
118 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     chemotaxis   3 terms 
  Biochemical function     protein binding     2 terms  


DOI no: 10.1002/pro.5560070221 Protein Sci 7:403-412 (1998)
PubMed id: 9521117  
Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability.
K.C.Usher, la Cruz, F.W.Dahlquist, R.V.Swanson, M.I.Simon, S.J.Remington.
The crystal structure of CheY protein from Thermotoga maritima has been determined in four crystal forms with and without Mg++ bound, at up to 1.9 A resolution. Structural comparisons with CheY from Escherichia coli shows substantial similarity in their folds, with some concerted changes propagating away from the active site that suggest how phosphorylated CheY, a signal transduction protein in bacterial chemotaxis, is recognized by its targets. A highly conserved segment of the protein (the "y-turn loop," residues 55-61), previously suggested to be a rigid recognition determinant, is for the first time seen in two alternative conformations in the different crystal structures. Although CheY from Thermotoga has much higher thermal stability than its mesophilic counterparts, comparison of structural features previously proposed to enhance thermostability such as hydrogen bonds, ion pairs, compactness, and hydrophobic surface burial would not suggest it to be so.

Literature references that cite this PDB file's key reference

  PubMed id Reference
18004790 M.Olufsen, E.Papaleo, A.O.Smalås, and B.O.Brandsdal (2008).
Ion pairs and their role in modulating stability of cold- and warm-active uracil DNA glycosylase.
  Proteins, 71, 1219-1230.  
18632584 T.A.Bharat, S.Eisenbeis, K.Zeth, and B.Höcker (2008).
A beta alpha-barrel built by the combination of fragments from different folds.
  Proc Natl Acad Sci U S A, 105, 9942-9947.
PDB code: 3cwo
18069884 A.Del Sol, and P.Carbonell (2007).
The Modular Organization of Domain Structures: Insights into Protein-Protein Binding.
  PLoS Comput Biol, 3, e239.  
17163981 E.Perez, and A.M.Stock (2007).
Characterization of the Thermotoga maritima chemotaxis methylation system that lacks pentapeptide-dependent methyltransferase CheR:MCP tethering.
  Mol Microbiol, 63, 363-378.  
17488848 T.Thireou, V.Atlamazoglou, M.Levakis, E.Eliopoulos, A.Hountas, G.Tsoucaris, and K.Bethanis (2007).
CrystTwiV: a webserver for automated phase extension and refinement in X-ray crystallography.
  Nucleic Acids Res, 35, W718-W722.  
16707700 E.Perez, H.Zheng, and A.M.Stock (2006).
Identification of methylation sites in Thermotoga maritima chemotaxis receptors.
  J Bacteriol, 188, 4093-4100.  
16120678 I.N.Berezovsky, and E.I.Shakhnovich (2005).
Physics and evolution of thermophilic adaptation.
  Proc Natl Acad Sci U S A, 102, 12742-12747.  
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
14581189 M.Torrez, M.Schultehenrich, and D.R.Livesay (2003).
Conferring thermostability to mesophilic proteins through optimized electrostatic surfaces.
  Biophys J, 85, 2845-2853.  
11787007 D.Pal, and P.Chakrabarti (2002).
On residues in the disallowed region of the Ramachandran map.
  Biopolymers, 63, 195-206.  
11331763 C.S.Bond, M.Kvaratskhelia, D.Richard, M.F.White, and W.N.Hunter (2001).
Structure of Hjc, a Holliday junction resolvase, from Sulfolobus solfataricus.
  Proc Natl Acad Sci U S A, 98, 5509-5514.
PDB code: 1hh1
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
10966457 A.M.Stock, V.L.Robinson, and P.N.Goudreau (2000).
Two-component signal transduction.
  Annu Rev Biochem, 69, 183-215.  
10944400 D.J.Rigden, L.V.Mello, and D.J.Bertioli (2000).
Structural modeling of a plant disease resistance gene product domain.
  Proteins, 41, 133-143.  
10591103 D.Maes, J.P.Zeelen, N.Thanki, N.Beaucamp, M.Alvarez, M.H.Thi, J.Backmann, J.A.Martial, L.Wyns, R.Jaenicke, and R.K.Wierenga (1999).
The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures.
  Proteins, 37, 441-453.
PDB code: 1b9b
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.