Dissemin is shutting down on January 1st, 2025

Published in

National Academy of Sciences, Proceedings of the National Academy of Sciences, 29(106), p. 11943-11947, 2009

DOI: 10.1073/pnas.0905081106

Links

Tools

Export citation

Search in Google Scholar

Insights into the molecular architecture of the 26S proteasome

Journal article published in 2009 by Stephan Nickell, Florian Beck, Sjors H. W. Scheres, Andreas Korinek, Friedrich Förster, Keren Lasker, Oana Mihalache, Na Sun, István Nagy, Andrej Sali, Jürgen M. Plitzko, Jose-Maria Carazo ORCID, Matthias Mann, Wolfgang Baumeister
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

Full text: Download

Red circle
Preprint: archiving forbidden
Green circle
Postprint: archiving allowed
Upload
Red circle
Published version: archiving forbidden
Policy details
Data provided by SHERPA/RoMEO

Abstract

Cryo-electron microscopy in conjunction with advanced image analysis was used to analyze the structure of the 26S proteasome and to elucidate its variable features. We have been able to outline the boundaries of the ATPase module in the "base" part of the regulatory complex that can vary in its position and orientation relative to the 20S core particle. This variation is consistent with the "wobbling" model that was previously proposed to explain the role of the regulatory complex in opening the gate in the alpha-rings of the core particle. In addition, a variable mass near the mouth of the ATPase ring has been identified as Rpn10, a multiubiquitin receptor, by correlating the electron microscopy data with quantitative mass spectrometry.