3HBT

The structure of native G-actin

3HBT の概要

• エントリーDOI: 10.2210/pdb3hbt/pdb
• 分子名称: Actin, SULFATE ION, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: g-actin, contractile protein, atp-binding, cytoskeleton, methylation, muscle protein, nucleotide-binding, phosphoprotein
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• 細胞内の位置: Cytoplasm, cytoskeleton: P68135
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 42518.96

構造登録者

Wang, H.,Robinson, R.C.,Burtnick, L.D. (登録日: 2009-05-05, 公開日: 2010-05-05, 最終更新日: 2023-11-01)

主引用文献

Wang, H.,Robinson, R.C.,Burtnick, L.D.
The structure of native G-actin
Cytoskeleton (Hoboken), 67:456-465, 2010

PubMed Abstract: Heat shock proteins act as cytoplasmic chaperones to ensure correct protein folding and prevent protein aggregation. The presence of stoichiometric amounts of one such heat shock protein, Hsp27, in supersaturated solutions of unmodified G-actin leads to crystallization, in preference to polymerization, of the actin. Hsp27 is not evident in the resulting crystal structure. Thus, for the first time, we present the structure of G-actin in a form that is devoid of polymerization-deterring chemical modifications or binding partners, either of which may alter its conformation. The structure contains a calcium ion and ATP within a closed nucleotide-binding cleft, and the D-loop is disordered. This native G-actin structure invites comparison with the current F-actin model in order to understand the structural implications for actin polymerization. In particular, this analysis suggests a mechanism by which the bound cation coordinates conformational change and ATP-hydrolysis.

PubMed: 20540085
DOI: 10.1002/cm.20458

実験手法

X-RAY DIFFRACTION (2.7 Å)