3RPG
Bmi1/Ring1b-UbcH5c complex structure
Summary for 3RPG
| Entry DOI | 10.2210/pdb3rpg/pdb |
| Related | 1X23 2CKL 2FUH 2H0D |
| Descriptor | Ubiquitin-conjugating enzyme E2 D3, Polycomb complex protein BMI-1, E3 ubiquitin-protein ligase RING2, ... (5 entities in total) |
| Functional Keywords | ubiquitin ligase, ligase |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cell membrane; Peripheral membrane protein: P61077 Nucleus: P35226 Q99496 |
| Total number of polymer chains | 3 |
| Total formula weight | 44262.56 |
| Authors | Bentley, M.L.,Dong, K.C.,Cochran, A.G. (deposition date: 2011-04-26, release date: 2011-08-17, Last modification date: 2023-09-13) |
| Primary citation | Bentley, M.L.,Corn, J.E.,Dong, K.C.,Phung, Q.,Cheung, T.K.,Cochran, A.G. Recognition of UbcH5c and the nucleosome by the Bmi1/Ring1b ubiquitin ligase complex. Embo J., 30:3285-3297, 2011 Cited by PubMed Abstract: The Polycomb repressive complex 1 (PRC1) mediates gene silencing, in part by monoubiquitination of histone H2A on lysine 119 (uH2A). Bmi1 and Ring1b are critical components of PRC1 that heterodimerize via their N-terminal RING domains to form an active E3 ubiquitin ligase. We have determined the crystal structure of a complex between the Bmi1/Ring1b RING-RING heterodimer and the E2 enzyme UbcH5c and find that UbcH5c interacts with Ring1b only, in a manner fairly typical of E2-E3 interactions. However, we further show that the Bmi1/Ring1b RING domains bind directly to duplex DNA through a basic surface patch unique to the Bmi1/Ring1b RING-RING dimer. Mutation of residues on this interaction surface leads to a loss of H2A ubiquitination activity. Computational modelling of the interface between Bmi1/Ring1b-UbcH5c and the nucleosome suggests that Bmi1/Ring1b interacts with both nucleosomal DNA and an acidic patch on histone H4 to achieve specific monoubiquitination of H2A. Our results point to a novel mechanism of substrate recognition, and control of product formation, by Bmi1/Ring1b. PubMed: 21772249DOI: 10.1038/emboj.2011.243 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6485 Å) |
Structure validation
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