Near-atomic resolution structural model of the yeast 26S proteasome
The 26S proteasome operates at the executive end of the ubiquitinproteasome pathway. Here, we present a cryo-EM structure of the Saccharomyces cerevisiae 26S proteasome at a resolution of 7.4 Å or 6.7 Å (Fourier-Shell Correlation of 0.5 or 0.3, respectively). We used this map in conjunction with mol...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2012-09, Vol.109 (37), p.14870-14875 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Beck, Florian Unverdorben, Pia Bohn, Stefan Schweitzer, Andreas Pfeifer, Günter Sakata, Eri Nickell, Stephan Plitzko, Jürgen M. Villa, Elizabeth Baumeister, Wolfgang Förster, Friedrich |
| description | The 26S proteasome operates at the executive end of the ubiquitinproteasome pathway. Here, we present a cryo-EM structure of the Saccharomyces cerevisiae 26S proteasome at a resolution of 7.4 Å or 6.7 Å (Fourier-Shell Correlation of 0.5 or 0.3, respectively). We used this map in conjunction with molecular dynamics-based flexible fitting to build a near-atomic resolution model of the holocomplex. The quality of the map allowed us to assign α-helices, the predominant secondary structure element of the regulatory particle subunits, throughout the entire map. We were able to determine the architecture of the Rpn8/Rpn11 heterodimer, which had hitherto remained elusive. The MPN domain of Rpn11 is positioned directly above the AAA-ATPase N-ring suggesting that Rpn11 deubiquitylates substrates immediately following commitment and prior to their unfolding by the AAA-ATPase module. The MPN domain of Rpn11 dimerizes with that of Rpn8 and the C-termini of both subunits form long helices, which are integral parts of a coiled-coil module. Together with the C-terminal helices of the six PCI-domain subunits they form a very large coiled-coil bundle, which appears to serve as a flexible anchoring device for all the lid subunits. |
| doi_str_mv | 10.1073/pnas.1213333109 |
| format | Article |
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Here, we present a cryo-EM structure of the Saccharomyces cerevisiae 26S proteasome at a resolution of 7.4 Å or 6.7 Å (Fourier-Shell Correlation of 0.5 or 0.3, respectively). We used this map in conjunction with molecular dynamics-based flexible fitting to build a near-atomic resolution model of the holocomplex. The quality of the map allowed us to assign α-helices, the predominant secondary structure element of the regulatory particle subunits, throughout the entire map. We were able to determine the architecture of the Rpn8/Rpn11 heterodimer, which had hitherto remained elusive. The MPN domain of Rpn11 is positioned directly above the AAA-ATPase N-ring suggesting that Rpn11 deubiquitylates substrates immediately following commitment and prior to their unfolding by the AAA-ATPase module. The MPN domain of Rpn11 dimerizes with that of Rpn8 and the C-termini of both subunits form long helices, which are integral parts of a coiled-coil module. 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| subjects | Adenosine triphosphatases Architectural models Architecture Biological Sciences Cells Cryoelectron Microscopy Crystal structure Crystals Electron microscopy Endopeptidases - chemistry Models, Molecular Molecular Dynamics Simulation Molecules proteasome endopeptidase complex Proteasome Endopeptidase Complex - chemistry Protein folding Protein Structure, Tertiary Proteins Rigid structures Saccharomyces cerevisiae Saccharomyces cerevisiae - chemistry Saccharomyces cerevisiae Proteins - chemistry Ubiquitins Yeast yeasts |
| title | Near-atomic resolution structural model of the yeast 26S proteasome |
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