Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 113, Issue 10, Pages 2642-2647Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1601561113
Keywords
protein degradation; proteasome; cryo-EM; structure
Categories
Funding
- National Natural Science Foundation of China [31321062, 31430020, 31100524, 31270764]
- NIH Grant [R37-GM043601]
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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.
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