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  Structural insights into the functional cycle of the ATPase module of the 26S proteasome

Wehmer, M., Rudack, T., Beck, F., Aufderheide, A., Pfeifer, G., Plitzko, J. M., et al. (2017). Structural insights into the functional cycle of the ATPase module of the 26S proteasome. Proceedings of the National Academy of Sciences of the United States of America, 114(6), 1305-1310. doi:10.1073/pnas.1621129114.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-DF99-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-DF9A-C
Genre: Journal Article

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 Creators:
Wehmer, Marc1, Author              
Rudack, Till2, Author
Beck, Florian1, Author              
Aufderheide, Antje1, Author              
Pfeifer, Günter1, Author              
Plitzko, Jürgen M.1, Author              
Förster, Friedrich1, Author              
Schulten, Klaus2, Author
Baumeister, Wolfgang1, Author              
Sakata, Eri1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2external, ou_persistent22              

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Free keywords: MOLECULAR-DYNAMICS; 20S PROTEASOME; CRYO-EM; THERMOPLASMA-ACIDOPHILUM; CRYOELECTRON MICROSCOPY; UBIQUITIN RECEPTOR; SUBUNIT; RESOLUTION; TRANSLOCATION; DEGRADATIONScience & Technology - Other Topics; 26S proteasome; cryo-electron microscopy; AAA(+) ATPase; integrative modeling; single-particle analysis;
 Abstract: In eukaryotic cells, the ubiquitin-proteasome system (UPS) is responsible for the regulated degradation of intracellular proteins. The 26S holocomplex comprises the core particle (CP), where proteolysis takes place, and one or two regulatory particles (RPs). The base of the RP is formed by a heterohexameric AAA(+) ATPase module, which unfolds and translocates substrates into the CP. Applying single-particle cryo-electron microscopy (cryo-EM) and image classification to samples in the presence of different nucleotides and nucleotide analogs, we were able to observe four distinct conformational states (s1 to s4). The resolution of the four conformers allowed for the construction of atomic models of the AAA(+) ATPase module as it progresses through the functional cycle. In a hitherto unobserved state (s4), the gate controlling access to the CP is open. The structures described in this study allow us to put forward a model for the 26S functional cycle driven by ATP hydrolysis.

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Language(s): eng - English
 Dates: 2017-01-232017-02
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: ISI: 000393422200039
DOI: 10.1073/pnas.1621129114
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proc. Acad. Sci. USA
  Other : Proc. Acad. Sci. U.S.A.
  Abbreviation : PNAS
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 114 (6) Sequence Number: - Start / End Page: 1305 - 1310 Identifier: ISSN: 0027-8424
CoNE: /journals/resource/954925427230