6U04
Crystal structure of human BRPF1 PZP bound to histone H3 tail
Summary for 6U04
| Entry DOI | 10.2210/pdb6u04/pdb |
| Descriptor | Histone H3.3,BRPF1, Peregrin, PRASEODYMIUM ION, ZINC ION, ... (4 entities in total) |
| Functional Keywords | epigenetics, nucleosome, dna binding, transcription |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 1 |
| Total formula weight | 22534.18 |
| Authors | Klein, B.J.,Kutateladze, T.G. (deposition date: 2019-08-13, release date: 2019-11-27, Last modification date: 2023-10-11) |
| Primary citation | Klein, B.J.,Cox, K.L.,Jang, S.M.,Cote, J.,Poirier, M.G.,Kutateladze, T.G. Molecular Basis for the PZP Domain of BRPF1 Association with Chromatin. Structure, 28:105-110.e3, 2020 Cited by PubMed Abstract: The assembly of human histone acetyltransferase MOZ/MORF complexes relies on the scaffolding bromodomain plant homeodomain (PHD) finger 1 (BRPF1) subunit. The PHD-zinc-knuckle-PHD module of BRPF1 (BRPF1) has been shown to associate with the histone H3 tail and DNA; however, the molecular mechanism underlying recognition of H3 and the relationship between the histone and DNA-binding activities remain unclear. In this study, we report the crystal structure of BRPF1 bound to the H3 tail and characterize the role of the bipartite interaction in the engagement of BRPF1 with the nucleosome core particle (NCP). We find that although both interactions of BRPF1 with the H3 tail and DNA are required for tight binding to NCP and for acetyltransferase function of the BRPF1-MORF-ING5-MEAF6 complex, binding to extranucleosomal DNA dominates. Our findings suggest that functionally active BRPF1 might be important in stabilization of the MOZ/MORF complexes at chromatin with accessible DNA. PubMed: 31711755DOI: 10.1016/j.str.2019.10.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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