5WVC

Structure of the CARD-CARD disk

Summary for 5WVC

• Entry DOI: 10.2210/pdb5wvc/pdb
• Descriptor: Apoptotic protease-activating factor 1, Caspase, IODIDE ION (3 entities in total)
• Functional Keywords: protein-protein interaction, signaling protein complex, apoptosis
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm : O14727
• Total number of polymer chains: 6
• Total formula weight: 86402.56

Authors

Lin, S.C.,Lo, Y.C.,Su, T.W. (deposition date: 2016-12-24, release date: 2017-04-19, Last modification date: 2024-11-06)

Primary citation

Su, T.W.,Yang, C.Y.,Kao, W.P.,Kuo, B.J.,Lin, S.M.,Lin, J.Y.,Lo, Y.C.,Lin, S.C.
Structural Insights into DD-Fold Assembly and Caspase-9 Activation by the Apaf-1 Apoptosome.
Structure, 25:407-420, 2017

PubMed Abstract: Death domain (DD)-fold assemblies play a crucial role in regulating the signaling to cell survival or death. Here we report the crystal structure of the caspase recruitment domain (CARD)-CARD disk of the human apoptosome. The structure surprisingly reveals that three 1:1 Apaf-1:procaspase-9 CARD protomers form a novel helical DD-fold assembly on the heptameric wheel-like platform of the apoptosome. The small-angle X-ray scattering and multi-angle light scattering data also support that three protomers could form an oligomeric complex similar to the crystal structure. Interestingly, the quasi-equivalent environment of CARDs could generate different quaternary CARD assemblies. We also found that the type II interaction is conserved in all DD-fold complexes, whereas the type I interaction is found only in the helical DD-fold assemblies. This study provides crucial insights into the caspase activation mechanism, which is tightly controlled by a sophisticated and highly evolved CARD assembly on the apoptosome, and also enables better understanding of the intricate DD-fold assembly.

PubMed: 28111022
DOI: 10.1016/j.str.2016.12.019

Experimental method

X-RAY DIFFRACTION (2.993 Å)