1U2V

Crystal structure of Arp2/3 complex with bound ADP and calcium

1U2V の概要

• エントリーDOI: 10.2210/pdb1u2v/pdb
• 関連するPDBエントリー: 1tyq
• 分子名称: Actin-Related Protein 3, Actin-Related Protein 2, Arp2/3 Complex 41Kda Subunit, ... (10 entities in total)
• 機能のキーワード: structural protein
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton (By similarity): P61157
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 225125.03

構造登録者

Nolen, B.J.,Littlefield, R.S.,Pollard, T.D. (登録日: 2004-07-20, 公開日: 2004-11-09, 最終更新日: 2024-03-13)

主引用文献

Nolen, B.J.,Littlefield, R.S.,Pollard, T.D.
Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP
Proc.Natl.Acad.Sci.Usa, 101:15627-15632, 2004

PubMed Abstract: 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.

PubMed: 15505213
DOI: 10.1073/pnas.0407149101

実験手法

X-RAY DIFFRACTION (2.55 Å)