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PDBsum entry 3o1h

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protein ligands Protein-protein interface(s) links
Signaling protein PDB id
3o1h

 

 

 

 

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Contents
Protein chains
270 a.a.
296 a.a.
Ligands
TMO
Waters ×71
PDB id:
3o1h
Name: Signaling protein
Title: Crystal structure of the tors sensor domain - tort complex in the presence of tmao
Structure: Sensor protein tors. Chain: a. Fragment: sensor domain (unp residues 51-322). Engineered: yes. Periplasmic protein tort. Chain: b. Fragment: unp residues 31-329. Engineered: yes
Source: Vibrio parahaemolyticus. Organism_taxid: 670. Strain: eb10. Gene: tors, vpa0675. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: tort, vpa0674.
Resolution:
3.10Å     R-factor:   0.218     R-free:   0.252
Authors: J.O.Moore,W.A.Hendrickson
Key ref: J.O.Moore and W.A.Hendrickson (2012). An asymmetry-to-symmetry switch in signal transmission by the histidine kinase receptor for TMAO. Structure, 20, 729-741. PubMed id: 22483119
Date:
21-Jul-10     Release date:   21-Dec-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q87ID1  (Q87ID1_VIBPA) -  histidine kinase from Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Seq:
Struc:
 
Seq:
Struc:
988 a.a.
270 a.a.*
Protein chain
Pfam   ArchSchema ?
Q87ID2  (Q87ID2_VIBPA) -  Periplasmic protein TorT from Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Seq:
Struc:
334 a.a.
296 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chain A: 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

 

 
    reference    
 
 
Structure 20:729-741 (2012)
PubMed id: 22483119  
 
 
An asymmetry-to-symmetry switch in signal transmission by the histidine kinase receptor for TMAO.
J.O.Moore, W.A.Hendrickson.
 
  ABSTRACT  
 
No abstract given.

 

 

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