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  Structure and Activity of the N-Terminal Substrate Recognition Domains in Proteasomal ATPases

Djuranovic, S., Hartmann, M., Habeck, M., Ursinus, A., Zwickl, P., Martin, J., et al. (2009). Structure and Activity of the N-Terminal Substrate Recognition Domains in Proteasomal ATPases. Molecular Cell, 34(5), 580-590. doi:10.1016/j.molcel.2009.04.030.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0013-C469-C Version Permalink: http://hdl.handle.net/21.11116/0000-0002-C03A-4
Genre: Journal Article

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 Creators:
Djuranovic, S1, Author
Hartmann, MD1, Author
Habeck, M1, Author              
Ursinus, A1, Author
Zwickl, P, Author
Martin, J1, Author
Lupas, AN1, Author
Zeth, K1, Author
Affiliations:
1Max Planck Institute for Developmental Biology, Max Planck Society, Max-Planck-Ring 5, 72076 Tübingen, DE, ou_2421691              

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 Abstract: The proteasome forms the core of the protein quality control system in archaea and eukaryotes and also occurs in one bacterial lineage, the Actinobacteria. Access to its proteolytic compartment is controlled by AAA ATPases, whose N-terminal domains (N domains) are thought to mediate substrate recognition. The N domains of an archaeal proteasomal ATPase, Archaeoglobus fulgidus PAN, and of its actinobacterial homolog, Rhodococcus erythropolis ARC, form hexameric rings, whose subunits consist of an N-terminal coiled coil and a C-terminal OB domain. In ARC-N, the OB domains are duplicated and form separate rings. PAN-N and ARC-N can act as chaperones, preventing the aggregation of heterologous proteins in vitro, and this activity is preserved in various chimeras, even when these include coiled coils and OB domains from unrelated proteins. The structures suggest a molecular mechanism for substrate processing based on concerted radial motions of the coiled coils relative to the OB rings.

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 Dates: 2009-06
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.1016/j.molcel.2009.04.030
BibTex Citekey: 5898
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Title: Molecular Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 34 (5) Sequence Number: - Start / End Page: 580 - 590 Identifier: ISSN: 1097-2765
CoNE: https://pure.mpg.de/cone/journals/resource/954925610929