3IZJ

Mm-cpn rls with ATP and AlFx

3IZJ の概要

• エントリーDOI: 10.2210/pdb3izj/pdb
• 関連するPDBエントリー: 3IZH 3IZI 3IZK 3IZL 3IZM 3IZN
• EMDBエントリー: 5246
• 分子名称: Chaperonin (1 entity in total)
• 機能のキーワード: mm-cpn, maripaludis, chaperonin, chaperone
• 由来する生物種: Methanococcus maripaludis
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 881911.38

構造登録者

Douglas, N.R.,Reissmann, S.,Zhang, J.,Chen, B.,Jakana, J.,Kumar, R.,Chiu, W.,Frydman, J. (登録日: 2010-10-29, 公開日: 2011-02-02, 最終更新日: 2024-02-21)

主引用文献

Douglas, N.R.,Reissmann, S.,Zhang, J.,Chen, B.,Jakana, J.,Kumar, R.,Chiu, W.,Frydman, J.
Dual Action of ATP Hydrolysis Couples Lid Closure to Substrate Release into the Group II Chaperonin Chamber.
Cell(Cambridge,Mass.), 144:240-252, 2011

PubMed Abstract: Group II chaperonins are ATP-dependent ring-shaped complexes that bind nonnative polypeptides and facilitate protein folding in archaea and eukaryotes. A built-in lid encapsulates substrate proteins within the central chaperonin chamber. Here, we describe the fate of the substrate during the nucleotide cycle of group II chaperonins. The chaperonin substrate-binding sites are exposed, and the lid is open in both the ATP-free and ATP-bound prehydrolysis states. ATP hydrolysis has a dual function in the folding cycle, triggering both lid closure and substrate release into the central chamber. Notably, substrate release can occur in the absence of a lid, and lid closure can occur without substrate release. However, productive folding requires both events, so that the polypeptide is released into the confined space of the closed chamber where it folds. Our results show that ATP hydrolysis coordinates the structural and functional determinants that trigger productive folding.

PubMed: 21241893
DOI: 10.1016/j.cell.2010.12.017

実験手法

ELECTRON MICROSCOPY (6.9 Å)