Structure of an endogenous yeast 26S proteasome reveals two major conformational states

文献类型： 外文期刊

第一作者： Luan, Bai

作者： Luan, Bai;Huang, Xiuliang;Wu, Jianping;Wang, Yiwei;Xue, Xiaobin;Yan, Chuangye;Wang, Jiawei;Shi, Yigong;Wang, Feng;Mei, Ziqing;Finley, Daniel J.

作者机构：

关键词： protein degradation;proteasome;cryo-EM;structure

期刊名称：PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA （ 影响因子：11.205； 五年影响因子：12.291 ）

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收录情况： SCI

摘要： 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-angstrom resolution. The fine features of the cryo-EM maps allow modeling of 18 sub-units 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-gamma S 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.

分类号： N

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