Crystal structure of Arp2/3 complex

R. C. Robinson, K. Turbedsky, D. A. Kaiser, J. B. Marchand, H. N. Higgs, S. Choe, T. D. Pollard

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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 α helices and have similarly folded amino-terminal α/β domains. ARPC1 p40 is a seven-blade β propeller with an insertion that may associate with the side of an actin filament. ARPC3 p21 and ARPC5 p16 are globular α-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.

Original languageEnglish
Pages (from-to)1679-1684
Number of pages6
JournalScience
Volume294
Issue number5547
DOIs
Publication statusPublished - Nov 23 2001

ASJC Scopus subject areas

  • General

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    Robinson, R. C., Turbedsky, K., Kaiser, D. A., Marchand, J. B., Higgs, H. N., Choe, S., & Pollard, T. D. (2001). Crystal structure of Arp2/3 complex. Science, 294(5547), 1679-1684. https://doi.org/10.1126/science.1066333