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Type: Journal article
Title: Structure of the Drosophila apoptosome at 6.9 Å resolution
Other Titles: Structure of the Drosophila apoptosome at 6.9 angstrom resolution
Author: Yuan, S.
Yu, X.
Topf, M.
Dorstyn, L.
Kumar, S.
Ludtke, S.
Akey, C.
Citation: Structure, 2011; 19(1):128-140
Publisher: Cell Press
Issue Date: 2011
ISSN: 0969-2126
Statement of
Shujun Yuan, Xinchao Yu, Maya Topf, Loretta Dorstyn, Sharad Kumar, Steven J. Ludtke and Christopher W. Akey
Abstract: 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.
Keywords: Animals
Drosophila melanogaster
Drosophila Proteins
Cryoelectron Microscopy
Protein Structure, Quaternary
Protein Structure, Secondary
Protein Structure, Tertiary
Structural Homology, Protein
Protein Binding
Protein Interaction Domains and Motifs
Protein Multimerization
Rights: © 2011 Elsevier
DOI: 10.1016/j.str.2010.10.009
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