1K8K

Crystal Structure of Arp2/3 Complex

Summary for 1K8K

• Entry DOI: 10.2210/pdb1k8k/pdb
• Descriptor: ACTIN-LIKE PROTEIN 3, ACTIN-LIKE PROTEIN 2, ARP2/3 COMPLEX 41 KDA SUBUNIT, ... (8 entities in total)
• Functional Keywords: beta-propeller, structural protein
• Biological source: Bos taurus (cattle); More
• Cellular location: Cytoplasm, cytoskeleton (By similarity): P61157 A7MB62 Q58CQ2 Q3MHR7 Q3T035 Q148J6 Q3SYX9
• Total number of polymer chains: 7
• Total formula weight: 224230.55

Authors

Robinson, R.C.,Turbedsky, K.,Kaiser, D.A.,Higgs, H.N.,Marchand, J.-B.,Choe, S.,Pollard, T.D. (deposition date: 2001-10-24, release date: 2001-12-07, Last modification date: 2024-02-07)

Primary citation

Robinson, R.C.,Turbedsky, K.,Kaiser, D.A.,Marchand, J.-B.,Higgs, H.N.,Choe, S.,Pollard, T.D.
Crystal Structure of Arp2/3 Complex
Science, 294:1679-1684, 2001

PubMed 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.

PubMed: 11721045
DOI: 10.1126/science.1066333

Experimental method

X-RAY DIFFRACTION (2 Å)