3LQQ
Structure of the CED-4 Apoptosome
3LQQ の概要
エントリーDOI | 10.2210/pdb3lqq/pdb |
関連するPDBエントリー | 2a5y 3lqr |
分子名称 | Cell death protein 4, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total) |
機能のキーワード | ced4, apoptosome, apoptosis, alternative splicing, atp-binding, mitochondrion, nucleotide-binding |
由来する生物種 | Caenorhabditis elegans (nematode) |
細胞内の位置 | Mitochondrion: P30429 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 126969.50 |
構造登録者 | |
主引用文献 | Qi, S.,Pang, Y.,Hu, Q.,Liu, Q.,Li, H.,Zhou, Y.,He, T.,Liang, Q.,Liu, Y.,Yuan, X.,Luo, G.,Li, H.,Wang, J.,Yan, N.,Shi, Y. Crystal structure of the Caenorhabditis elegans apoptosome reveals an octameric assembly of CED-4. Cell(Cambridge,Mass.), 141:446-457, 2010 Cited by PubMed 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. PubMed: 20434985DOI: 10.1016/j.cell.2010.03.017 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.534 Å) |
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