@article{168386,
  keywords = {Animals, X-Ray Diffraction, Models, Molecular, Crystallography, X-Ray, Caenorhabditis elegans, Amino Acid Sequence, Sequence Alignment, Caenorhabditis elegans Proteins, Calcium-Binding Proteins, Caspases, Apoptosomes, Apoptotic Protease-Activating Factor 1},
  author = {Shiqian Qi and Yuxuan Pang and Qi Hu and Qun Liu and Hua Li and Yulian Zhou and Tianxi He and Qionglin Liang and Yexing Liu and Xiaoqiu Yuan and Guoan Luo and Huilin Li and Jiawei Wang and Nieng Yan and Yigong Shi},
  title = {Crystal structure of the Caenorhabditis elegans apoptosome reveals an octameric assembly of CED-4},
  abstract = {<p>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.</p>
},
  year = {2010},
  journal = {Cell},
  volume = {141},
  pages = {446-57},
  month = {04/2010},
  issn = {1097-4172},
  doi = {10.1016/j.cell.2010.03.017},
  language = {eng},
}