1k8k: Difference between revisions

Revision as of 22:26, 2 May 2008

Crystal Structure of Arp2/3 Complex

OverviewOverview

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.

About this StructureAbout this Structure

1K8K is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of Arp2/3 complex., Robinson RC, Turbedsky K, Kaiser DA, Marchand JB, Higgs HN, Choe S, Pollard TD, Science. 2001 Nov 23;294(5547):1679-84. PMID:11721045 Page seeded by OCA on Fri May 2 22:26:13 2008

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OCA

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 '''Crystal Structure of Arp2/3 Complex'''
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 22:26:13 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:44:53 2008''