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- W2118084489 abstract "The CED-4 homo-oligomer or apoptosome is required for initiation of programmed cell death in Caenorhabditis elegans by facilitating autocatalytic activation of the CED-3 caspase zymogen. How the CED-4 apoptosome assembles and activates CED-3 remains enigmatic. Here we report the crystal structure of the complete CED-4 apoptosome and show that it consists of eight CED-4 molecules, organized as a tetramer of an asymmetric dimer via a previously unreported interface among AAA(+) ATPases. These eight CED-4 molecules form a funnel-shaped structure. The mature CED-3 protease is monomeric in solution and forms an active holoenzyme with the CED-4 apoptosome, within which the protease activity of CED-3 is markedly stimulated. Unexpectedly, the octameric CED-4 apoptosome appears to bind only two, not eight, molecules of mature CED-3. The structure of the CED-4 apoptosome reveals shared principles for the NB-ARC family of AAA(+) ATPases and suggests a mechanism for the activation of CED-3." @default.
- W2118084489 created "2016-06-24" @default.
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- W2118084489 date "2010-04-01" @default.
- W2118084489 modified "2023-10-14" @default.
- W2118084489 title "Crystal Structure of the Caenorhabditis elegans Apoptosome Reveals an Octameric Assembly of CED-4" @default.
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- W2118084489 doi "https://doi.org/10.1016/j.cell.2010.03.017" @default.
- W2118084489 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20434985" @default.
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