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Robert C. Robinson,*Kirsi Turbedsky,*Donald A. Kaiser,Jean-Baptiste Marchand,Henry N. Higgs,§Senyon Choe,Thomas D. Pollard¶
We determined a crystal structure of bovine Arp2/3 complex, an
assembly of seven proteins that initiates actin polymerizationin
eukaryotic cells, at 2.0 angstrom resolution. Actin-relatedprotein 2 (Arp2) and Arp3 are folded like actin, with distinctivesurface
features. Subunits ARPC2 p34 and ARPC4 p20 in the coreof the complex
associate through long carboxyl-terminal helicesand have similarly
folded amino-terminal / domains. ARPC1 p40is a seven-blade propeller with an insertion that may associatewith the side of an
actin filament. ARPC3 p21 and ARPC5 p16 areglobular -helical
subunits. We predict that WASp/Scar proteinsactivate Arp2/3 complex by
bringing Arp2 into proximity with Arp3for nucleation of a branch on
the side of a preexisting actinfilament.
Structural Biology Laboratory, Salk Institute for Biological
Studies, 10010 North Torrey Pines Road, La Jolla, CA 92037, USA.
*
These authors contributed equally to this work.
Present address: Department of Medical Biochemistry
and Microbiology, Uppsala University, Uppsala, Sweden.
Present address: Avidis, Biopole Clermont-Limagne, 63 360 Saint Beauzire, France.
§
Present address: Department of Biochemistry, Dartmouth
College, Hanover, NH 03755, USA.
Present address: Department of Molecular, Cellular, and
Developmental Biology, Yale University, New Haven, CT 06520, USA.
¶
To whom correspondence should be addressed. E-mail:
thomas.pollard{at}yale.edu
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