PDBsum entry 2vcp

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protein ligands metals Protein-protein interface(s) links
Structural protein PDB id
Protein chains
371 a.a.
20 a.a. *
ATP ×2
_CA ×2
* Residue conservation analysis
PDB id:
Name: Structural protein
Title: Crystal structure of n-wasp vc domain in complex with skeletal actin
Structure: Actin, alpha skeletal muscle. Chain: a, b. Fragment: residues 3-377. Synonym: alpha-actin-1. Neural wiskott-aldrich syndrome protein. Chain: d, e. Fragment: wh2 1,2 and c domain, residues 392-484. Synonym: n-wasp. Engineered: yes
Source: Oryctolagus cuniculus. Rabbit. Organism_taxid: 9986. Tissue: skeletal muscle. Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
3.20Å     R-factor:   0.275     R-free:   0.331
Authors: J.F.Gaucher,D.Didry,M.F.Carlier
Key ref: J.F.Gaucher et al. (2012). Interactions of isolated C-terminal fragments of neural Wiskott-Aldrich syndrome protein (N-WASP) with actin and Arp2/3 complex. J Biol Chem, 287, 34646-34659. PubMed id: 22847007 DOI: 10.1074/jbc.M112.394361
26-Sep-07     Release date:   04-Nov-08    
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Protein chains
Pfam   ArchSchema ?
P68135  (ACTS_RABIT) -  Actin, alpha skeletal muscle
377 a.a.
371 a.a.*
Protein chains
Pfam   ArchSchema ?
O00401  (WASL_HUMAN) -  Neural Wiskott-Aldrich syndrome protein
505 a.a.
20 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   5 terms 
  Biological process     actin filament organization   3 terms 
  Biochemical function     nucleotide binding     6 terms  


DOI no: 10.1074/jbc.M112.394361 J Biol Chem 287:34646-34659 (2012)
PubMed id: 22847007  
Interactions of isolated C-terminal fragments of neural Wiskott-Aldrich syndrome protein (N-WASP) with actin and Arp2/3 complex.
J.F.Gaucher, C.Maugé, D.Didry, B.Guichard, L.Renault, M.F.Carlier.
Wiskott-Aldrich syndrome proteins (WASP) are a family of proteins that all catalyze actin filament branching with the Arp2/3 complex in a variety of actin-based motile processes. The constitutively active C-terminal domain, called VCA, harbors one or more WASP homology 2 (WH2) domains that bind G-actin, whereas the CA extension binds the Arp2/3 complex. The VCA·actin·Arp2/3 entity associates with a mother filament to form a branched junction from which a daughter filament is initiated. The number and function of WH2-bound actin(s) in the branching process are not known, and the stoichiometry of the VCA·actin·Arp2/3 complex is debated. We have expressed the tandem WH2 repeats of N-WASP, either alone (V) or associated with the C (VC) and CA (VCA) extensions. We analyzed the structure of actin in complex with V, VC, and VCA using protein crystallography and hydrodynamic and spectrofluorimetric methods. The partial crystal structure of the VC·actin 1:1 complex shows two actins in the asymmetric unit with extensive actin-actin contacts. In solution, each of the two WH2 domains in V, VC, and VCA binds G-actin in 1:2 complexes that participate in barbed end assembly. V, VC, and VCA enhance barbed end depolymerization like profilin but neither nucleate nor sever filaments, in contrast with other WH2 repeats. VCA binds the Arp2/3 complex in a 1:1 complex even in the presence of a large excess of VCA. VCA·Arp2/3 binds one actin in a latrunculin A-sensitive fashion, in a 1:1:1 complex, indicating that binding of the second actin to VCA is weakened in the ternary complex.

Literature references that cite this PDB file's key reference

  PubMed id Reference
23212475 J.D.Rotty, C.Wu, and J.E.Bear (2012).
New insights into the regulation and cellular functions of the ARP2/3 complex.
  Nat Rev Mol Cell Biol, 14, 7.  
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