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PDBsum entry 4a2m

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protein ligands Protein-protein interface(s) links
Transcription PDB id
4a2m

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
741 a.a.
Ligands
NGS-GCD ×4
PDB id:
4a2m
Name: Transcription
Title: Structure of the periplasmic domain of the heparin and heparan sulphate sensing hybrid two component system bt4663 in apo and ligand bound forms
Structure: Two-component system sensor histidine kinase/response. Chain: a, b, c, d. Fragment: periplasmic domain, residues 1-787. Synonym: bt_4663. Engineered: yes
Source: Bacteroides thetaiotaomicron. Organism_taxid: 226186. Strain: vpi-5482. Atcc: 29148. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
3.40Å     R-factor:   0.269     R-free:   0.286
Authors: E.C.Lowe,A.Basle,M.Czjzek,S.J.Firbank,D.N.Bolam
Key ref: E.C.Lowe et al. (2012). A scissor blade-like closing mechanism implicated in transmembrane signaling in a Bacteroides hybrid two-component system. Proc Natl Acad Sci U S A, 109, 7298-7303. PubMed id: 22532667
Date:
27-Sep-11     Release date:   02-May-12    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q89YR8  (Q89YR8_BACTN) -  histidine kinase from Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1353 a.a.
741 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: 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    
 
 
Proc Natl Acad Sci U S A 109:7298-7303 (2012)
PubMed id: 22532667  
 
 
A scissor blade-like closing mechanism implicated in transmembrane signaling in a Bacteroides hybrid two-component system.
E.C.Lowe, A.Baslé, M.Czjzek, S.J.Firbank, D.N.Bolam.
 
  ABSTRACT  
 
No abstract given.

 

 

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