2P9P
Crystal Structure of bovine Arp2/3 complex co-crystallized with ADP
Summary for 2P9P
Entry DOI | 10.2210/pdb2p9p/pdb |
Related | 2P9I 2P9K 2P9L 2P9N 2P9S 2P9U |
Descriptor | Actin-like protein 3, Actin-like protein 2, Actin-related protein 2/3 complex subunit 1B, ... (9 entities in total) |
Functional Keywords | actin, wd repeat, complex, structural protein |
Biological source | Bos taurus (cattle) More |
Cellular location | Cytoplasm, cytoskeleton : P61157 A7MB62 Q58CQ2 Q3MHR7 Q3T035 Q148J6 Q3SYX9 |
Total number of polymer chains | 7 |
Total formula weight | 225125.03 |
Authors | Nolen, B.J.,Pollard, T.D. (deposition date: 2007-03-26, release date: 2007-05-29, Last modification date: 2024-02-21) |
Primary citation | Nolen, 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: 17499050DOI: 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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