Summary for 4V4L
| Entry DOI | 10.2210/pdb4v4l/pdb |
| EMDB information | 5235 |
| Descriptor | Apaf-1 related killer DARK, MAGNESIUM ION, 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE (3 entities in total) |
| Functional Keywords | drosophila apoptosome, apoptosis, programmed cell death |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 16 |
| Total formula weight | 1979376.29 |
| Authors | Yuan, S.,Topf, M.,Akey, C.W.,Ludtke, S.J. (deposition date: 2010-10-04, release date: 2014-07-09, Last modification date: 2024-02-28) |
| Primary citation | Yuan, S.,Yu, X.,Topf, M.,Dorstyn, L.,Kumar, S.,Ludtke, S.J.,Akey, C.W. Structure of the Drosophila apoptosome at 6.9 angstrom resolution Structure, 19:128-140, 2011 Cited by PubMed Abstract: The Drosophila Apaf-1 related killer forms an apoptosome in the intrinsic cell death pathway. In this study we show that Dark forms a single ring when initiator procaspases are bound. This Dark-Dronc complex cleaves DrICE efficiently; hence, a single ring represents the Drosophila apoptosome. We then determined the 3D structure of a double ring at ∼6.9 Å resolution and created a model of the apoptosome. Subunit interactions in the Dark complex are similar to those in Apaf-1 and CED-4 apoptosomes, but there are significant differences. In particular, Dark has "lost" a loop in the nucleotide-binding pocket, which opens a path for possible dATP exchange in the apoptosome. In addition, caspase recruitment domains (CARDs) form a crown on the central hub of the Dark apoptosome. This CARD geometry suggests that conformational changes will be required to form active Dark-Dronc complexes. When taken together, these data provide insights into apoptosome structure, function, and evolution. PubMed: 21220123DOI: 10.1016/j.str.2010.10.009 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.9 Å) |
Structure validation
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