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Free keywords:
REGULATORY PARTICLE; UBIQUITIN SYSTEM; CRYO-EM; SUBSTRATE TRANSLOCATION;
MOLECULAR ARCHITECTURE; DEGRADATION; RESOLUTION; MECHANISM; MODEL; YEASTBiochemistry & Molecular Biology; Cell Biology; 26S proteasome; Cryoelectron microscopy; Single particle analysis;
Structural biology; AAA plus ATPase;
Abstract:
There is growing appreciation for the fundamental role of structural dynamics in the function of macromolecules. In particular, the 26S proteasome, responsible for selective protein degradation in an ATP dependent manner, exhibits dynamic conformational changes that enable substrate processing. Recent cryo-electron microscopy (cryo-EM) work has revealed the conformational dynamics of the 26S proteasome and established the function of the different conformational states. Technological advances such as direct electron detectors and image processing algorithms allowed resolving the structure of the proteasome at atomic resolution. Here we will review those studies and discuss their contribution to our understanding of proteasome function. (C) 2016 The Authors. Published by Elsevier Ltd.
