2p9p
Crystal Structure of bovine Arp2/3 complex co-crystallized with ADPCrystal Structure of bovine Arp2/3 complex co-crystallized with ADP
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedATP is required for nucleation of actin filament branches by Arp2/3 complex, but the influence of ATP binding and hydrolysis are poorly understood. We determined crystal structures of bovine Arp2/3 complex cocrystallized with various bound adenine nucleotides and cations. Nucleotide binding favors closure of the nucleotide-binding cleft of Arp3, but no large-scale conformational changes in the complex. Thus, ATP binding does not directly activate Arp2/3 complex but is part of a network of interactions that contribute to nucleation. We compared nucleotide-induced conformational changes of residues lining the cleft in Arp3 and actin structures to construct a movie depicting the proposed ATPase cycle for the actin family. Chemical crosslinking stabilized subdomain 1 of Arp2, revealing new electron density for 69 residues in this subdomain. Steric clashes with Arp3 appear to be responsible for intrinsic disorder of subdomains 1 and 2 of Arp2 in inactive Arp2/3 complex. Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2/3 complex.,Nolen BJ, Pollard TD Mol Cell. 2007 May 11;26(3):449-57. PMID:17499050[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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