Insights into the molecular architecture of the 26S proteasome

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, Matthias Mann, Wolfgang Baumeister

Research output: Contribution to journalArticleAcademicpeer-review


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.

Original languageEnglish
Pages (from-to)11943-7
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number29
Publication statusPublished - 21 Jul 2009
Externally publishedYes


  • Adenosine Triphosphatases
  • Animals
  • Cryoelectron Microscopy
  • Drosophila melanogaster
  • Mass Spectrometry
  • Models, Molecular
  • Proteasome Endopeptidase Complex
  • Protein Subunits
  • Protein Transport


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