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  Structure of the 26S proteasome with ATP-gamma S bound provides insights into the mechanism of nucleotide-dependent substrate translocation

Sledz, P., Unverdorben, P., Beck, F., Pfeifer, G., Schweitzer, A., Förster, F., et al. (2013). Structure of the 26S proteasome with ATP-gamma S bound provides insights into the mechanism of nucleotide-dependent substrate translocation. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 110(18), 7264-7269. doi:10.1073/pnas.1305782110.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0013-B25B-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0013-B25D-8
Genre: Journal Article

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 Creators:
Sledz, Pawel1, Author              
Unverdorben, Pia1, Author              
Beck, Florian1, Author              
Pfeifer, Günter1, Author              
Schweitzer, Andreas1, Author              
Förster, Friedrich1, Author              
Baumeister, Wolfgang1, Author              
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1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: REGULATORY PARTICLE; METHANOCALDOCOCCUS-JANNASCHII; MOLECULAR ARCHITECTURE; 20S PROTEASOME; AAA; ATPASES; PROTEIN; MICROSCOPY; RESOLUTION; MACHINEAAA ATPase; ubiquitin-proteasome pathway; hybrid methods in structural biology;
 Abstract: The 26S proteasome is a 2.5-MDa, ATP-dependent multisubunit proteolytic complex that processively destroys proteins carrying a degradation signal. The proteasomal ATPase heterohexamer is a key module of the 19S regulatory particle; it unfolds substrates and translocates them into the 20S core particle where degradation takes place. We used cryoelectron microscopy single-particle analysis to obtain insights into the structural changes of 26S proteasome upon the binding and hydrolysis of ATP. The ATPase ring adopts at least two distinct helical staircase conformations dependent on the nucleotide state. The transition from the conformation observed in the presence of ATP to the predominant conformation in the presence of ATP-gamma S induces a sliding motion of the ATPase ring over the 20S core particle ring leading to an alignment of the translocation channels of the ATPase and the core particle gate, a conformational state likely to facilitate substrate translocation. Two types of inter-subunit modules formed by the large ATPase domain of one ATPase subunit and the small ATPase domain of its neighbor exist. They resemble the contacts observed in the crystal structures of ClpX and proteasome-activating nucleotidase, respectively. The ClpX-like contacts are positioned consecutively and give rise to helical shape in the hexamer, whereas the proteasome-activating nucleotidase-like contact is required to close the ring. Conformational switching between these forms allows adopting different helical conformations in different nucleotide states. We postulate that ATP hydrolysis by the regulatory particle ATPase (Rpt) 5 subunit initiates a cascade of conformational changes, leading to pulling of the substrate, which is primarily executed by Rpt1, Rpt2, and Rpt6.

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Language(s): eng - English
 Dates: 2013-04-30
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000318682300041
DOI: 10.1073/pnas.1305782110
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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: 110 (18) Sequence Number: - Start / End Page: 7264 - 7269 Identifier: ISSN: 0027-8424