Summary for 8ATX
| Entry DOI | 10.2210/pdb8atx/pdb |
| Related | 8ATU |
| EMDB information | 15668 |
| Descriptor | Baculoviral IAP repeat-containing protein 6, ZINC ION (2 entities in total) |
| Functional Keywords | e3 ubiquitin ligase, e2/e3 hybrid, inhibitor of apoptosis protein, ligase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 1064148.82 |
| Authors | Ehrmann, J.F.,Grabarczyk, D.B.,Clausen, T. (deposition date: 2022-08-24, release date: 2023-02-15, Last modification date: 2024-07-24) |
| Primary citation | Ehrmann, J.F.,Grabarczyk, D.B.,Heinke, M.,Deszcz, L.,Kurzbauer, R.,Hudecz, O.,Shulkina, A.,Gogova, R.,Meinhart, A.,Versteeg, G.A.,Clausen, T. Structural basis for regulation of apoptosis and autophagy by the BIRC6/SMAC complex. Science, 379:1117-1123, 2023 Cited by PubMed Abstract: Inhibitor of apoptosis proteins (IAPs) bind to pro-apoptotic proteases, keeping them inactive and preventing cell death. The atypical ubiquitin ligase BIRC6 is the only essential IAP, additionally functioning as a suppressor of autophagy. We performed a structure-function analysis of BIRC6 in complex with caspase-9, HTRA2, SMAC, and LC3B, which are critical apoptosis and autophagy proteins. Cryo-electron microscopy structures showed that BIRC6 forms a megadalton crescent shape that arcs around a spacious cavity containing receptor sites for client proteins. Multivalent binding of SMAC obstructs client binding, impeding ubiquitination of both autophagy and apoptotic substrates. On the basis of these data, we discuss how the BIRC6/SMAC complex can act as a stress-induced hub to regulate apoptosis and autophagy drivers. PubMed: 36758105DOI: 10.1126/science.ade8873 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7 Å) |
Structure validation
Download full validation report
