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  Structure of the human 26S proteasome at a resolution of 3.9 angstrom

Schweitzer, A., Aufderheide, A., Rudack, T., Beck, F., Pfeifer, G., Plitzko, J. M., et al. (2016). Structure of the human 26S proteasome at a resolution of 3.9 angstrom. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 113(28), 7816-7821. doi:10.1073/pnas.1608050113.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-1EDB-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-1EDC-2
Genre: Journal Article

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 Creators:
Schweitzer, Andreas1, Author              
Aufderheide, Antje1, Author              
Rudack, Till2, Author
Beck, Florian1, Author              
Pfeifer, Günter1, Author              
Plitzko, Jürgen M.1, Author              
Sakata, Eri1, Author              
Schulten, Klaus2, Author
Förster, Friedrich1, 3, Author              
Baumeister, Wolfgang1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2external, ou_persistent22              
3Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565148              

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Free keywords: MOLECULAR-DYNAMICS SIMULATIONS; CRYO-EM STRUCTURE; REGULATORY PARTICLE; 20S PROTEASOME; UBIQUITIN RECEPTOR; CRYSTAL-STRUCTURE; DEGRADATION; SUBUNIT; DEUBIQUITINATION; SOFTWAREproteostasis; cryo-electron microscopy; AAA-ATPase; integrative modeling;
 Abstract: Protein degradation in eukaryotic cells is performed by the Ubiquitin-Proteasome System (UPS). The 26S proteasome holocomplex consists of a core particle (CP) that proteolytically degrades polyubiquitylated proteins, and a regulatory particle (RP) containing the AAA-ATPase module. This module controls access to the proteolytic chamber inside the CP and is surrounded by non-ATPase subunits (Rpns) that recognize substrates and deubiquitylate them before unfolding and degradation. The architecture of the 26S holocomplex is highly conserved between yeast and humans. The structure of the human 26S holocomplex described here reveals previously unidentified features of the AAA-ATPase heterohexamer. One subunit, Rpt6, has ADP bound, whereas the other five have ATP in their binding pockets. Rpt6 is structurally distinct from the other five Rpt subunits, most notably in its pore loop region. For Rpns, the map reveals two main, previously undetected, features: the C terminus of Rpn3 protrudes into the mouth of the ATPase ring; and Rpn1 and Rpn2, the largest proteasome subunits, are linked by an extended connection. The structural features of the 26S proteasome observed in this study are likely to be important for coordinating the proteasomal subunits during substrate processing.

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Language(s): eng - English
 Dates: 2016
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000379694100046
DOI: 10.1073/pnas.1608050113
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Title: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Source Genre: Journal
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Publ. Info: 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA : NATL ACAD SCIENCES
Pages: - Volume / Issue: 113 (28) Sequence Number: - Start / End Page: 7816 - 7821 Identifier: ISSN: 0027-8424