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PDBsum entry 3mpl

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protein ligands links
Signaling protein PDB id
3mpl

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
233 a.a. *
Ligands
EDO ×2
Waters ×82
* Residue conservation analysis
PDB id:
3mpl
Name: Signaling protein
Title: Crystal structure of bordetella pertussis bvgs vft2 domain (double mutant f375e/q461e)
Structure: Virulence sensor protein bvgs. Chain: a. Fragment: unp residues 287-542. Engineered: yes. Mutation: yes
Source: Bordetella pertussis. Organism_taxid: 257313. Strain: tohamai. Gene: bp1877, bvgs. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.10Å     R-factor:   0.191     R-free:   0.245
Authors: J.Herrou,C.Bompard,R.Wintjens,E.Dupre,E.Willery,V.Villeret,C.Locht, R.Antoine,F.Jacob-Dubuisson
Key ref: J.Herrou et al. (2010). Periplasmic domain of the sensor-kinase BvgS reveals a new paradigm for the Venus flytrap mechanism. Proc Natl Acad Sci U S A, 107, 17351-17355. PubMed id: 20855615
Date:
27-Apr-10     Release date:   06-Oct-10    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P16575  (BVGS_BORPE) -  Virulence sensor protein BvgS from Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1238 a.a.
233 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 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 107:17351-17355 (2010)
PubMed id: 20855615  
 
 
Periplasmic domain of the sensor-kinase BvgS reveals a new paradigm for the Venus flytrap mechanism.
J.Herrou, C.Bompard, R.Wintjens, E.Dupré, E.Willery, V.Villeret, C.Locht, R.Antoine, F.Jacob-Dubuisson.
 
  ABSTRACT  
 
No abstract given.

 

 

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