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TitleStructure of an apoptosome-procaspase-9 CARD complex.
Journal, issue, pagesStructure, Vol. 18, Issue 5, Page 571-583, Year 2010
Publish dateMay 12, 2010
AuthorsShujun Yuan / Xinchao Yu / Maya Topf / Steven J Ludtke / Xiaodong Wang / Christopher W Akey /
PubMed AbstractApaf-1 coassembles with cytochrome c to form the apoptosome, which then binds and activates procaspase-9 (pc-9). We removed pc-9 catalytic domains from the holoapoptosome by site-directed ...Apaf-1 coassembles with cytochrome c to form the apoptosome, which then binds and activates procaspase-9 (pc-9). We removed pc-9 catalytic domains from the holoapoptosome by site-directed thrombinolysis. A structure of the resulting apoptosome-pc-9 CARD complex was then determined at approximately 9.5 A resolution. In our model, the central hub is constructed like other AAA+ protein rings but also contains novel features. At higher radius, the regulatory region of each Apaf-1 is comprised of tandem seven and eight blade beta-propellers with cytochrome c docked between them. Remarkably, Apaf-1 CARDs are disordered in the ground state. During activation, each Apaf-1 CARD interacts with a pc-9 CARD and these heterodimers form a flexibly tethered "disk" that sits above the central hub. When taken together, the data reveal conformational changes during Apaf-1 assembly that allow pc-9 activation. The model also provides a plausible explanation for the effects of NOD mutations that have been mapped onto the central hub.
External linksStructure / PubMed:20462491 / PubMed Central
MethodsEM (single particle)
Resolution9.5 Å
Structure data

EMDB-5186:
Structure of an apoptosome-procaspase-9 CARD complex
Method: EM (single particle) / Resolution: 9.5 Å

Source
  • Homo sapiens (human)
  • Bos taurus (cattle)

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