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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2010-3-15
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pubmed:databankReference |
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pubmed:abstractText |
The proteasome is an abundant protease that is critically important for numerous cellular pathways. Proteasomes are activated in vitro by three known classes of proteins/complexes, including Blm10/PA200. Here, we report a 3.4 A resolution crystal structure of a proteasome-Blm10 complex, which reveals that Blm10 surrounds the proteasome entry pore in the 1.2 MDa complex to form a largely closed dome that is expected to restrict access of potential substrates. This architecture and the observation that Blm10 induces a disordered proteasome gate structure challenge the assumption that Blm10 functions as an activator of proteolysis in vivo. The Blm10 C terminus binds in the same manner as seen for 11S activators and inferred for 19S/PAN activators and indicates a unified model for gate opening. We also demonstrate that Blm10 acts to maintain mitochondrial function. Consistent with the structural data, the C-terminal residues of Blm10 are needed for this activity.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-11081519,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-11917093,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-12015144,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-12093752,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-12535522,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-12941688,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-12973301,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-13421693,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-15099583,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-15449308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-15653075,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-15778719,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-15916965,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-16581775,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-16952374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-17523843,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-17803938,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-17911101,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-18172023,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-18471981,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-18796432,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-18845680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-18927584,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-7725097,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-7725107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-9087403,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20227375-9501171
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1097-4164
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pubmed:author |
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pubmed:copyrightInfo |
(c) 2010 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
12
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
728-35
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pubmed:dateRevised |
2011-7-26
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pubmed:meshHeading |
pubmed-meshheading:20227375-Amino Acid Sequence,
pubmed-meshheading:20227375-Catalytic Domain,
pubmed-meshheading:20227375-Crystallography, X-Ray,
pubmed-meshheading:20227375-Genotype,
pubmed-meshheading:20227375-Mitochondria,
pubmed-meshheading:20227375-Models, Molecular,
pubmed-meshheading:20227375-Molecular Sequence Data,
pubmed-meshheading:20227375-Mutation,
pubmed-meshheading:20227375-Phenotype,
pubmed-meshheading:20227375-Proteasome Endopeptidase Complex,
pubmed-meshheading:20227375-Protein Binding,
pubmed-meshheading:20227375-Protein Conformation,
pubmed-meshheading:20227375-Reactive Oxygen Species,
pubmed-meshheading:20227375-Saccharomyces cerevisiae,
pubmed-meshheading:20227375-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:20227375-Structure-Activity Relationship
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pubmed:year |
2010
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pubmed:articleTitle |
Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening.
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pubmed:affiliation |
Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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