Crystal structure of Arp2/3 complex

Citation
Rc. Robinson et al., Crystal structure of Arp2/3 complex, SCIENCE, 294(5547), 2001, pp. 1679-1684
Citations number
37
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Multidisciplinary,Multidisciplinary,Multidisciplinary
Journal title
SCIENCE
ISSN journal
0036-8075 → ACNP
Volume
294
Issue
5547
Year of publication
2001
Pages
1679 - 1684
Database
ISI
SICI code
0036-8075(20011123)294:5547<1679:CSOAC>2.0.ZU;2-2
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 ARPC 4 p20 in the core of the complex associate through long carboxyl-terminal a helices and have similarly folded amino-terminal alpha/beta domains. ARPC1 p40 is a seven-blade beta propeller with an insertion that may associate w ith the side of an actin filament. ARPC3 p21 and ARPC5 p16 are globular alp ha -helical subunits. We predict that WASp/Scar proteins activate Arp2/3 co mplex by bringing Arp2 into proximity with Arp3 for nucleation of a branch on the side of a preexisting actin filament.