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-Structure paper
Title | Structure of an endogenous yeast 26S proteasome reveals two major conformational states. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 113, Issue 10, Page 2642-2647, Year 2016 |
Publish date | Mar 8, 2016 |
Authors | Bai Luan / Xiuliang Huang / Jianping Wu / Ziqing Mei / Yiwei Wang / Xiaobin Xue / Chuangye Yan / Jiawei Wang / Daniel J Finley / Yigong Shi / Feng Wang / |
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 ...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. |
External links | Proc Natl Acad Sci U S A / PubMed:26929360 / PubMed Central |
Methods | EM (single particle) |
Resolution | 4.6 - 8.7 Å |
Structure data | EMDB-6574: Cryo-EM map of yeast 26S proteasome in M1 state derived from Titan dataset EMDB-6575: Cryo-EM map of yeast 26S proteasome in M2 state derived from Titan dataset EMDB-6576: EMDB-6577: EMDB-6578: EMDB-6579: |
Source |
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Keywords | HYDROLASE / protein complex |