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2P9P

Crystal Structure of bovine Arp2/3 complex co-crystallized with ADP

Summary for 2P9P
Entry DOI10.2210/pdb2p9p/pdb
Related2P9I 2P9K 2P9L 2P9N 2P9S 2P9U
DescriptorActin-like protein 3, Actin-like protein 2, Actin-related protein 2/3 complex subunit 1B, ... (9 entities in total)
Functional Keywordsactin, wd repeat, complex, structural protein
Biological sourceBos taurus (cattle)
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Cellular locationCytoplasm, cytoskeleton : P61157 A7MB62 Q58CQ2 Q3MHR7 Q3T035 Q148J6 Q3SYX9
Total number of polymer chains7
Total formula weight225125.03
Authors
Nolen, B.J.,Pollard, T.D. (deposition date: 2007-03-26, release date: 2007-05-29, Last modification date: 2024-02-21)
Primary citationNolen, B.J.,Pollard, T.D.
Insights into the Influence of Nucleotides on Actin Family Proteins from Seven Structures of Arp2/3 Complex.
Mol.Cell, 26:449-457, 2007
Cited by
PubMed Abstract: 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.
PubMed: 17499050
DOI: 10.1016/j.molcel.2007.04.017
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

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