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PDBsum entry 2f9z

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protein Protein-protein interface(s) links
Signaling protein PDB id
2f9z
Jmol
Contents
Protein chains
193 a.a. *
190 a.a. *
154 a.a. *
Waters ×392
* Residue conservation analysis
PDB id:
2f9z
Name: Signaling protein
Title: Complex between the chemotaxis deamidase ched and the chemot phosphatase chec from thermotoga maritima
Structure: Chemotaxis protein chec. Chain: a, b. Engineered: yes. Protein (chemotaxis methylation protein). Chain: c, d. Engineered: yes
Source: Thermotoga maritima. Organism_taxid: 243274. Strain: msb8. Gene: tm0904. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: tm0903.
Biol. unit: Tetramer (from PQS)
Resolution:
2.40Å     R-factor:   0.211     R-free:   0.275
Authors: X.Chao,S.Y Park,A.M.Bilwes,B.R.Crane
Key ref:
X.Chao et al. (2006). A receptor-modifying deamidase in complex with a signaling phosphatase reveals reciprocal regulation. Cell, 124, 561-571. PubMed id: 16469702 DOI: 10.1016/j.cell.2005.11.046
Date:
06-Dec-05     Release date:   06-Jun-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9X006  (CHEC_THEMA) -  CheY-P phosphatase CheC
Seq:
Struc:
205 a.a.
193 a.a.
Protein chain
Pfam   ArchSchema ?
Q9X006  (CHEC_THEMA) -  CheY-P phosphatase CheC
Seq:
Struc:
205 a.a.
190 a.a.
Protein chains
Pfam   ArchSchema ?
Q9X005  (CHED_THEMA) -  Chemoreceptor glutamine deamidase CheD
Seq:
Struc:
157 a.a.
154 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 2: Chains C, D: E.C.3.1.1.61  - Protein-glutamate methylesterase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein L-glutamate O5-methyl ester + H2O = protein L-glutamate + methanol
Protein L-glutamate O(5)-methyl ester
+ H(2)O
= protein L-glutamate
+ methanol
   Enzyme class 3: Chains C, D: E.C.3.5.1.44  - Protein-glutamine glutaminase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein L-glutamine + H2O = protein L-glutamate + NH3
Protein L-glutamine
+ H(2)O
= protein L-glutamate
+ NH(3)
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   2 terms 
  Biochemical function     hydrolase activity     3 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.cell.2005.11.046 Cell 124:561-571 (2006)
PubMed id: 16469702  
 
 
A receptor-modifying deamidase in complex with a signaling phosphatase reveals reciprocal regulation.
X.Chao, T.J.Muff, S.Y.Park, S.Zhang, A.M.Pollard, G.W.Ordal, A.M.Bilwes, B.R.Crane.
 
  ABSTRACT  
 
Signal transduction underlying bacterial chemotaxis involves excitatory phosphorylation and feedback control through deamidation and methylation of sensory receptors. The structure of a complex between the signal-terminating phosphatase, CheC, and the receptor-modifying deamidase, CheD, reveals how CheC mimics receptor substrates to inhibit CheD and how CheD stimulates CheC phosphatase activity. CheD resembles other cysteine deamidases from bacterial pathogens that inactivate host Rho-GTPases. CheD not only deamidates receptor glutamine residues contained within a conserved structural motif but also hydrolyzes glutamyl-methyl-esters at select regulatory positions. Substituting Gln into the receptor motif of CheC turns the inhibitor into a CheD substrate. Phospho-CheY, the intracellular signal and CheC target, stabilizes the CheC:CheD complex and reduces availability of CheD. A point mutation that dissociates CheC from CheD impairs chemotaxis in vivo. Thus, CheC incorporates an element of an upstream receptor to influence both its own effect on receptor output and that of its binding partner, CheD.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. Substrate Sites for CheD
Figure 4.
Figure 4. The CheC:CheD Complex Mimics the Receptor:CheD Interaction
 
  The above figures are reprinted by permission from Cell Press: Cell (2006, 124, 561-571) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21255112 K.J.Watts, B.L.Taylor, and M.S.Johnson (2011).
PAS/poly-HAMP signalling in Aer-2, a soluble haem-based sensor.
  Mol Microbiol, 79, 686-699.  
21283116 S.L.Porter, G.H.Wadhams, and J.P.Armitage (2011).
Signal processing in complex chemotaxis pathways.
  Nat Rev Microbiol, 9, 153-165.  
20722598 B.A.Wilson, and M.Ho (2010).
Recent insights into Pasteurella multocida toxin and other G-protein-modulating bacterial toxins.
  Future Microbiol, 5, 1185-1201.  
20355710 J.Bhatnagar, P.P.Borbat, A.M.Pollard, A.M.Bilwes, J.H.Freed, and B.R.Crane (2010).
Structure of the ternary complex formed by a chemotaxis receptor signaling domain, the CheA histidine kinase, and the coupling protein CheW as determined by pulsed dipolar ESR spectroscopy.
  Biochemistry, 49, 3824-3841.  
20133180 R.E.Silversmith (2010).
Auxiliary phosphatases in two-component signal transduction.
  Curr Opin Microbiol, 13, 177-183.  
20080618 Y.Pazy, M.A.Motaleb, M.T.Guarnieri, N.W.Charon, R.Zhao, and R.E.Silversmith (2010).
Identical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrate.
  Proc Natl Acad Sci U S A, 107, 1924-1929.
PDB code: 3hzh
19379070 J.R.Kirby (2009).
Chemotaxis-like regulatory systems: unique roles in diverse bacteria.
  Annu Rev Microbiol, 63, 45-59.  
18844997 H.T.Tran, J.Krushkal, F.M.Antommattei, D.R.Lovley, and R.M.Weis (2008).
Comparative genomics of Geobacter chemotaxis genes reveals diverse signaling function.
  BMC Genomics, 9, 471.  
18990184 T.J.Muff, and G.W.Ordal (2008).
The diverse CheC-type phosphatases: chemotaxis and beyond.
  Mol Microbiol, 70, 1054-1061.  
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.  
17628132 K.Wuichet, R.P.Alexander, and I.B.Zhulin (2007).
Comparative genomic and protein sequence analyses of a complex system controlling bacterial chemotaxis.
  Methods Enzymol, 422, 1.  
17299051 R.P.Alexander, and I.B.Zhulin (2007).
Evolutionary genomics reveals conserved structural determinants of signaling and adaptation in microbial chemoreceptors.
  Proc Natl Acad Sci U S A, 104, 2885-2890.  
17177603 R.Zhao, D.Oxley, T.S.Smith, G.A.Follows, A.R.Green, and D.R.Alexander (2007).
DNA damage-induced Bcl-xL deamidation is mediated by NHE-1 antiport regulated intracellular pH.
  PLoS Biol, 5, e1.  
17908686 T.J.Muff, and G.W.Ordal (2007).
The CheC phosphatase regulates chemotactic adaptation through CheD.
  J Biol Chem, 282, 34120-34128.  
17675386 T.J.Muff, R.M.Foster, P.J.Liu, and G.W.Ordal (2007).
CheX in the three-phosphatase system of bacterial chemotaxis.
  J Bacteriol, 189, 7007-7013.  
16707700 E.Perez, H.Zheng, and A.M.Stock (2006).
Identification of methylation sites in Thermotoga maritima chemotaxis receptors.
  J Bacteriol, 188, 4093-4100.  
16882724 S.Y.Park, B.Lowder, A.M.Bilwes, D.F.Blair, and B.R.Crane (2006).
Structure of FliM provides insight into assembly of the switch complex in the bacterial flagella motor.
  Proc Natl Acad Sci U S A, 103, 11886-11891.
PDB code: 2hp7
16622408 S.Y.Park, P.P.Borbat, G.Gonzalez-Bonet, J.Bhatnagar, A.M.Pollard, J.H.Freed, A.M.Bilwes, and B.R.Crane (2006).
Reconstruction of the chemotaxis receptor-kinase assembly.
  Nat Struct Mol Biol, 13, 400-407.
PDB codes: 2ch4 2ch7
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.