6KRD

TRiC at 0.05 mM ADP-AlFx, Conformation 4, 0.05-C4

6KRD の概要

• エントリーDOI: 10.2210/pdb6krd/pdb
• EMDBエントリー: 0756
• 分子名称: T-complex protein 1 subunit alpha, T-complex protein 1 subunit beta, T-complex protein 1 subunit delta, ... (8 entities in total)
• 機能のキーワード: chaperonin tric/cct, allosteric network, atpase cycle, conformational landscape, cryo-em, chaperone
• 由来する生物種: Saccharomyces cerevisiae S288C (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 955870.85

構造登録者

Jin, M.,Cong, Y. (登録日: 2019-08-21, 公開日: 2019-09-18, 最終更新日: 2025-07-02)

主引用文献

Jin, M.,Han, W.,Liu, C.,Zang, Y.,Li, J.,Wang, F.,Wang, Y.,Cong, Y.
An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.
Proc.Natl.Acad.Sci.USA, 116:19513-19522, 2019

PubMed Abstract: TRiC/CCT assists the folding of ∼10% of cytosolic proteins through an ATP-driven conformational cycle and is essential in maintaining protein homeostasis. Here, we determined an ensemble of cryo-electron microscopy (cryo-EM) structures of yeast TRiC at various nucleotide concentrations, with 4 open-state maps resolved at near-atomic resolutions, and a closed-state map at atomic resolution, revealing an extra layer of an unforeseen N-terminal allosteric network. We found that, during TRiC ring closure, the CCT7 subunit moves first, responding to nucleotide binding; CCT4 is the last to bind ATP, serving as an ATP sensor; and CCT8 remains ADP-bound and is hardly involved in the ATPase-cycle in our experimental conditions; overall, yeast TRiC consumes nucleotide in a 2-ring positively coordinated manner. Our results depict a thorough picture of the TRiC conformational landscape and its allosteric transitions from the open to closed states in more structural detail and offer insights into TRiC subunit specificity in ATP consumption and ring closure, and potentially in substrate processing.

PubMed: 31492816
DOI: 10.1073/pnas.1903976116

実験手法

ELECTRON MICROSCOPY (4.38 Å)