spacer
spacer

PDBsum entry 3tj6

Go to PDB code: 
protein Protein-protein interface(s) links
Protein binding/toxin PDB id
3tj6
Jmol
Contents
Protein chains
253 a.a.
23 a.a.
Waters ×141
PDB id:
3tj6
Name: Protein binding/toxin
Title: Human vinculin head domain (vh1, residues 1-258) in complex vinculin binding site of the surface cell antigen 4 (sca4-v residues 812-835) from rickettsia rickettsii
Structure: Vinculin. Chain: a. Synonym: metavinculin. Engineered: yes. Antigenic heat-stable 120 kda protein. Chain: b. Fragment: unp residues 812-834. Synonym: 120 kda antigen, protein ps 120, ps120. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: vcl. Expressed in: escherichia coli. Expression_system_taxid: 562. Rickettsia rickettsii. Organism_taxid: 452659. Strain: iowa.
Resolution:
2.76Å     R-factor:   0.196     R-free:   0.235
Authors: H.Park,J.H.Lee,E.Gouin,P.Cossart,T.Izard
Key ref: H.Park et al. (2011). The rickettsia surface cell antigen 4 applies mimicry to bind to and activate vinculin. J Biol Chem, 286, 35096-35103. PubMed id: 21841197 DOI: 10.1074/jbc.M111.263855
Date:
23-Aug-11     Release date:   07-Sep-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P18206  (VINC_HUMAN) -  Vinculin
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1134 a.a.
253 a.a.
Protein chain
Pfam   ArchSchema ?
B0BXR4  (B0BXR4_RICRO) -  Antigenic heat-stable 120 kDa protein
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1024 a.a.
23 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     actin cytoskeleton   1 term 
  Biological process     cell adhesion   1 term 
  Biochemical function     structural molecule activity     1 term  

 

 
DOI no: 10.1074/jbc.M111.263855 J Biol Chem 286:35096-35103 (2011)
PubMed id: 21841197  
 
 
The rickettsia surface cell antigen 4 applies mimicry to bind to and activate vinculin.
H.Park, J.H.Lee, E.Gouin, P.Cossart, T.Izard.
 
  ABSTRACT  
 
No abstract given.