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Complex (chemotaxis/transferase) PDB id
1bdj
Jmol
Contents
Protein chains
128 a.a. *
117 a.a. *
Ligands
SO4
Waters ×44
* Residue conservation analysis
PDB id:
1bdj
Name: Complex (chemotaxis/transferase)
Title: Complex structure of hpt domain and chey
Structure: Chey. Chain: a. Synonym: chemotaxis protein chey. Engineered: yes. Other_details: the response regulator. Aerobic respiration control sensor protein arcb. Chain: b. Fragment: hpt domain, the histidine-containing phosphotransfer domain.
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: bl21. Expression_system_variant: dz225.
Resolution:
2.68Å     R-factor:   0.183     R-free:   0.250
Authors: M.Kato,T.Mizuno,T.Shimizu,T.Hakoshima
Key ref:
M.Kato et al. (1999). Structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor protein ArcB complexed with the chemotaxis response regulator CheY. Acta Crystallogr D Biol Crystallogr, 55, 1257-1263. PubMed id: 10393292 DOI: 10.1107/S0907444999005053
Date:
10-May-98     Release date:   11-May-99    
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.
Protein chain
Pfam   ArchSchema ?
P0AEC3  (ARCB_ECOLI) -  Aerobic respiration control sensor protein ArcB
Seq:
Struc: 		 
Seq:
Struc: 		778 a.a.
117 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chain B: 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   2 terms 
  Biological process     intracellular signal transduction   7 terms 
  Biochemical function     signal transducer activity     6 terms  

 

 
    reference    
 
 
DOI no: 10.1107/S0907444999005053 Acta Crystallogr D Biol Crystallogr 55:1257-1263 (1999)
PubMed id: 10393292  
 
 
Structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor protein ArcB complexed with the chemotaxis response regulator CheY.
M.Kato, T.Shimizu, T.Mizuno, T.Hakoshima.
 
  ABSTRACT  
 
The three-dimensional structure of the HPt domain of ArcB complexed with CheY has been determined using the molecular-replacement method. The structure was refined to a crystallographic R factor of 18.3% at 2.68 A resolution. The final model included 1899 protein atoms (117 residues from the HPt domain and 128 residues from CheY), one sulfate ion and 44 solvent molecules. In the crystal, CheY molecules stacked along the a axis of the cell with no interactions between neighbouring rows and the HPt domain bridged the CheY molecules. The phosphodonor residue His715 was fully exposed to the solvent region, even though the HPt domain was in contact with four molecules of CheY. CheY showed significant conformational change. This indicates that the HPt domain has a rigid structure when complexed with CheY.
 
  Selected figure(s)  
 
Figure 4.
Figure 4 Stereo diagram showing the superposition of C[ ]traces of the HPt-CheY complex, the 2.06 Å HPt domain, apo-CheY and Mg^2+-CheY. The complex including contact region #2 is shown. The HPt domain and CheY in the complex are shown as thin lines, the 2.06 Å HPt domain and apo-CheY as thick lines and Mg^2+-CheY as dashed lines. The white ball-and-stick models are the residues Lys658, His715, Phe14, Asp57, Tyr106 and Lys109 and the SO^2-[4] ion in the complex. The grey ball-and-stick models are the residue Asp57 and the Mg^2+ ion in Mg^2+-CheY. The black ball-and-stick model is the SO^2-[4] ion in apo-CheY. 		Figure 6.
Figure 6 A graphic representation of the hydrogen bonds to SO^2-[4] ions. (a) The SO^2-[4] ion in the complex structure and (b) the SO^2-[4] ion in the apo-CheY structure. Hydrogen bonds are shown as dashed lines with their distance in Å. The residues whose side chains participate in the hydrogen bonding are represented as rectangles and the residues whose main chains participate in the hydrogen bonding are represented as ovals.
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1999, 55, 1257-1263) copyright 1999.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19246748 R.Shrivastava, A.K.Ghosh, and A.K.Das (2009).
Intra- and intermolecular domain interactions among novel two-component system proteins coded by Rv0600c, Rv0601c and Rv0602c of Mycobacterium tuberculosis.
  Microbiology, 155, 772-779.  
14563873 J.G.Smith, J.A.Latiolais, G.P.Guanga, S.Citineni, R.E.Silversmith, and R.B.Bourret (2003).
Investigation of the role of electrostatic charge in activation of the Escherichia coli response regulator CheY.
  J Bacteriol, 185, 6385-6391.  
  12372152 P.M.Wolanin, P.A.Thomason, and J.B.Stock (2002).
Histidine protein kinases: key signal transducers outside the animal kingdom.
  Genome Biol, 3, REVIEWS3013.  
10837243 J.Stock, and S.Da Re (2000).
Signal transduction: response regulators on and off.
  Curr Biol, 10, R420-R424.  
  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
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