Crystal structure of Arp2/3 complex
- PMID: 11721045
- DOI: 10.1126/science.1066333
Crystal structure of Arp2/3 complex
Abstract
We determined a crystal structure of bovine Arp2/3 complex, an assembly of seven proteins that initiates actin polymerization in eukaryotic cells, at 2.0 angstrom resolution. Actin-related protein 2 (Arp2) and Arp3 are folded like actin, with distinctive surface features. Subunits ARPC2 p34 and ARPC4 p20 in the core of the complex associate through long carboxyl-terminal alpha helices and have similarly folded amino-terminal alpha/beta domains. ARPC1 p40 is a seven-blade beta propeller with an insertion that may associate with the side of an actin filament. ARPC3 p21 and ARPC5 p16 are globular alpha-helical subunits. We predict that WASp/Scar proteins activate Arp2/3 complex by bringing Arp2 into proximity with Arp3 for nucleation of a branch on the side of a preexisting actin filament.
Comment in
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Structure. Action at the Y-branch.Science. 2001 Nov 23;294(5547):1660-1. doi: 10.1126/science.1067619. Science. 2001. PMID: 11721036 No abstract available.
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