2VCP
Crystal structure of N-Wasp VC domain in complex with skeletal actin
Summary for 2VCP
| Entry DOI | 10.2210/pdb2vcp/pdb |
| Related | 1ALM 1ATN 1EQY 1ESV 1H1V 1IJJ 1J6Z 1KXP 1LCU 1LOT 1M8Q 1MA9 1MVW 1NWK 1O18 1O19 1O1A 1O1B 1O1C 1O1D 1O1E 1O1F 1O1G 1P8Z 1QZ5 1QZ6 1RDW 1RFQ 1RGI 1S22 1SQK 1T44 1UY5 1WUA 1Y64 2A3Z 2A40 2A41 2A42 2A5X 2ASM 2ASO 2ASP 2D1K 2FF3 2FF6 2FXU 2V39 |
| Descriptor | ACTIN, ALPHA SKELETAL MUSCLE, NEURAL WISKOTT-ALDRICH SYNDROME PROTEIN, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total) |
| Functional Keywords | actin-binding, transcription, muscle protein, nucleotide-binding, transcription regulation, methylation, atp-binding, cytoskeleton, phosphorylation, structural protein, wh2, wasp, actin, nucleus, twinning |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Total number of polymer chains | 4 |
| Total formula weight | 104499.89 |
| Authors | Gaucher, J.F.,Didry, D.,Carlier, M.F. (deposition date: 2007-09-26, release date: 2008-11-04, Last modification date: 2023-12-13) |
| Primary citation | Gaucher, J.F.,Mauge, C.,Didry, D.,Guichard, B.,Renault, L.,Carlier, M.F. 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, 2012 Cited by PubMed Abstract: 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. PubMed: 22847007DOI: 10.1074/jbc.M112.394361 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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