Source:http://linkedlifedata.com/resource/pubmed/id/21220123
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2011-1-11
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pubmed:databankReference | |
pubmed:abstractText |
The Drosophila Apaf-1 related killer forms an apoptosome in the intrinsic cell death pathway. In this study we show that Dark forms a single ring when initiator procaspases are bound. This Dark-Dronc complex cleaves DrICE efficiently; hence, a single ring represents the Drosophila apoptosome. We then determined the 3D structure of a double ring at ?6.9 Å resolution and created a model of the apoptosome. Subunit interactions in the Dark complex are similar to those in Apaf-1 and CED-4 apoptosomes, but there are significant differences. In particular, Dark has "lost" a loop in the nucleotide-binding pocket, which opens a path for possible dATP exchange in the apoptosome. In addition, caspase recruitment domains (CARDs) form a crown on the central hub of the Dark apoptosome. This CARD geometry suggests that conformational changes will be required to form active Dark-Dronc complexes. When taken together, these data provide insights into apoptosome structure, function, and evolution.
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pubmed:grant | |
pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apoptosomes,
http://linkedlifedata.com/resource/pubmed/chemical/Ark protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ice protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Nc protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1878-4186
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2011 Elsevier Ltd. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
12
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
128-40
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pubmed:dateRevised |
2011-6-6
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pubmed:meshHeading |
pubmed-meshheading:21220123-Animals,
pubmed-meshheading:21220123-Apoptosomes,
pubmed-meshheading:21220123-Caspases,
pubmed-meshheading:21220123-Cryoelectron Microscopy,
pubmed-meshheading:21220123-Drosophila Proteins,
pubmed-meshheading:21220123-Drosophila melanogaster,
pubmed-meshheading:21220123-Protein Binding,
pubmed-meshheading:21220123-Protein Interaction Domains and Motifs,
pubmed-meshheading:21220123-Protein Multimerization,
pubmed-meshheading:21220123-Protein Structure, Quaternary,
pubmed-meshheading:21220123-Protein Structure, Secondary,
pubmed-meshheading:21220123-Protein Structure, Tertiary,
pubmed-meshheading:21220123-Structural Homology, Protein
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pubmed:year |
2011
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pubmed:articleTitle |
Structure of the Drosophila apoptosome at 6.9 å resolution.
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pubmed:affiliation |
Department of Physiology and Biophysics, Boston University School of Medicine, 700 Albany Street, Boston, MA 02118, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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