期刊
MOLECULAR CELL
卷 26, 期 3, 页码 449-457出版社
CELL PRESS
DOI: 10.1016/j.molcel.2007.04.017
关键词
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资金
- NIGMS NIH HHS [P01GM066311, F32 GM074374, F32 GM074374-02, P01 GM066311-05, P01 GM066311, F32GM074374] Funding Source: Medline
ATP 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.
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