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TitleNear-atomic resolution structural model of the yeast 26S proteasome.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 109, Issue 37, Page 14870-14875, Year 2012
Publish dateSep 11, 2012
AuthorsFlorian Beck / Pia Unverdorben / Stefan Bohn / Andreas Schweitzer / Günter Pfeifer / Eri Sakata / Stephan Nickell / Jürgen M Plitzko / Elizabeth Villa / Wolfgang Baumeister / Friedrich Förster /
PubMed AbstractThe 26S proteasome operates at the executive end of the ubiquitin-proteasome pathway. Here, we present a cryo-EM structure of the Saccharomyces cerevisiae 26S proteasome at a resolution of 7.4 Å or ...The 26S proteasome operates at the executive end of the ubiquitin-proteasome 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.
External linksProc Natl Acad Sci U S A / PubMed:22927375 / PubMed Central
MethodsEM (single particle)
Resolution7.4 Å
Structure data

EMDB-2165:
Cryo-EM reconstruction of the yeast 26S proteasome
Method: EM (single particle) / Resolution: 7.4 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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