3JCP

Structure of yeast 26S proteasome in M2 state derived from Titan dataset

これはPDB形式変換不可エントリーです。

3JCP の概要

• エントリーDOI: 10.2210/pdb3jcp/pdb
• EMDBエントリー: 6575
• 分子名称: Proteasome subunit beta type-6, Proteasome subunit alpha type-3, Proteasome subunit alpha type-4, ... (33 entities in total)
• 機能のキーワード: protein complex, hydrolase
• 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: 47
• 化学式量合計: 1692659.85

構造登録者

Luan, B.,Huang, X.L.,Wu, J.P.,Shi, Y.G.,Wang, F. (登録日: 2016-01-06, 公開日: 2016-06-15, 最終更新日: 2024-03-20)

主引用文献

Luan, B.,Huang, X.L.,Wu, J.P.,Shi, Y.G.,Wang, F.
Structure of an endogenous yeast 26S proteasome reveals two major conformational states.
Proc.Natl.Acad.Sci.USA, 113:2642-2647, 2016

PubMed Abstract: The eukaryotic proteasome mediates degradation of polyubiquitinated proteins. Here we report the single-particle cryoelectron microscopy (cryo-EM) structures of the endogenous 26S proteasome from Saccharomyces cerevisiae at 4.6- to 6.3-Å resolution. The fine features of the cryo-EM maps allow modeling of 18 subunits in the regulatory particle and 28 in the core particle. The proteasome exhibits two distinct conformational states, designated M1 and M2, which correspond to those reported previously for the proteasome purified in the presence of ATP-γS and ATP, respectively. These conformations also correspond to those of the proteasome in the presence and absence of exogenous substrate. Structure-guided biochemical analysis reveals enhanced deubiquitylating enzyme activity of Rpn11 upon assembly of the lid. Our structures serve as a molecular basis for mechanistic understanding of proteasome function.

PubMed: 26929360
DOI: 10.1073/pnas.1601561113

実験手法

ELECTRON MICROSCOPY (4.6 Å)