3LQR

Structure of CED-4:CED-3 complex

Summary for 3LQR

• Entry DOI: 10.2210/pdb3lqr/pdb
• Related: 2a5y 3lqq
• Descriptor: Cell death protein 4, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: ced-4, ced-3, apoptosis, apoptosome, alternative splicing, atp-binding, mitochondrion, nucleotide-binding
• Biological source: Caenorhabditis elegans (nematode)
• Cellular location: Mitochondrion: P30429
• Total number of polymer chains: 2
• Total formula weight: 126969.50

Authors

Qi, S.,Pang, Y.,Shi, Y.,Yan, N. (deposition date: 2010-02-09, release date: 2010-04-28, Last modification date: 2023-11-01)

Primary citation

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

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: 20434985
DOI: 10.1016/j.cell.2010.03.017

Experimental method

X-RAY DIFFRACTION (3.896 Å)