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Near-atomic resolution structural model of the yeast 26S proteasome

Beck, Florian ; Unverdorben, Pia ; Bohn, Stefan ; Schweitzer, Andreas ; Pfeifer, Günter ; Sakata, Eri ; Nickell, Stephan ; Plitzko, Jürgen M. ; Villa, Elizabeth ; Baumeister, Wolfgang ; Förster, Friedrich

Proceedings of the National Academy of Sciences - PNAS, 2012-09, Vol.109 (37), p.14870-14875 [Periódico revisado por pares]

United States: National Academy of Sciences

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Título:
Near-atomic resolution structural model of the yeast 26S proteasome
Autor: Beck, Florian ; Unverdorben, Pia ; Bohn, Stefan ; Schweitzer, Andreas ; Pfeifer, Günter ; Sakata, Eri ; Nickell, Stephan ; Plitzko, Jürgen M. ; Villa, Elizabeth ; Baumeister, Wolfgang ; Förster, Friedrich
Assuntos: 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 - chemistry ; Protein folding ; Protein Structure, Tertiary ; Proteins ; Rigid structures ; Saccharomyces cerevisiae - chemistry ; Saccharomyces cerevisiae Proteins - chemistry ; Ubiquitins ; Yeast
É parte de: Proceedings of the National Academy of Sciences - PNAS, 2012-09, Vol.109 (37), p.14870-14875
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
2Present address: Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520.
1F.B. and P.U. contributed equally to this work.
Author contributions: J.M.P., E.V., W.B., and F.F. designed research; F.B., P.U., S.B., A.S., G.P., E.S., S.N., J.M.P., and E.V. performed research; F.B., P.U., S.B., and F.F. analyzed data; and F.B., P.U., W.B., and F.F. wrote the paper.
Contributed by Wolfgang Baumeister, August 3, 2012 (sent for review July 20, 2012)
3Present address: BioSciences Division, Carl Zeiss Microscopy GmbH, 73447 Oberkochen, Germany.
Descrição: 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.
Editor: United States: National Academy of Sciences
Idioma: Inglês

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Near-atomic resolution structural model of the yeast 26S proteasome

Beck, Florian ; Unverdorben, Pia ; Bohn, Stefan ; Schweitzer, Andreas ; Pfeifer, Günter ; Sakata, Eri ; Nickell, Stephan ; Plitzko, Jürgen M. ; Villa, Elizabeth ; Baumeister, Wolfgang ; Förster, Friedrich

United States: National Academy of Sciences

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