1tyq
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Crystal structure of Arp2/3 complex with bound ATP and calcium
OverviewOverview
Actin-related protein (Arp) 2/3 complex stimulates formation of actin, filaments at the leading edge of motile cells. Nucleation of filaments, depends on hydrolysis of ATP bound to Arp2. Here we report crystal, structures of Arp2/3 complex with bound ATP or ADP. The nucleotides are, immobilized on the face of subdomains 3 and 4 of Arp2, whereas subdomains, 1 and 2 are flexible and absent from the electron density maps. This, flexibility may explain why Arp2 does not hydrolyze ATP until the complex, is activated. ATP stabilizes a relatively closed conformation of Arp3 with, the gamma-phosphate bridging loops from opposite sides of the cleft. ADP, binds Arp3 in a unique conformation that favors an open cleft, revealing a, conformational change that may occur in actin and Arps when ATP is, hydrolyzed and phosphate dissociates. These structures provide the an, opportunity to compare all nucleotide-binding states in an actin-related, protein and give insights into the function of both the Arp2/3 complex and, actin.
About this StructureAbout this Structure
1TYQ is a Single protein structure of sequence from Bos taurus with CA and ATP as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP., Nolen BJ, Littlefield RS, Pollard TD, Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15627-32. Epub 2004 Oct 25. PMID:15505213
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