5ERC
X-ray crystal structure of BRPF1 PZP domain
Summary for 5ERC
Entry DOI | 10.2210/pdb5erc/pdb |
Descriptor | Peregrin, ZINC ION, CALCIUM ION, ... (4 entities in total) |
Functional Keywords | reader domain, methyllysine, dna, h3 histone, transcription |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 1 |
Total formula weight | 20035.84 |
Authors | Klein, B.J.,Andrews, F.H.,Kutateladze, T.G. (deposition date: 2015-11-13, release date: 2015-12-30, Last modification date: 2024-03-06) |
Primary citation | Klein, B.J.,Muthurajan, U.M.,Lalonde, M.E.,Gibson, M.D.,Andrews, F.H.,Hepler, M.,Machida, S.,Yan, K.,Kurumizaka, H.,Poirier, M.G.,Cote, J.,Luger, K.,Kutateladze, T.G. Bivalent interaction of the PZP domain of BRPF1 with the nucleosome impacts chromatin dynamics and acetylation. Nucleic Acids Res., 44:472-484, 2016 Cited by PubMed Abstract: BRPF1 (bromodomain PHD finger 1) is a core subunit of the MOZ histone acetyltransferase (HAT) complex, critical for normal developmental programs and implicated in acute leukemias. BRPF1 contains a unique assembly of zinc fingers, termed a PZP domain, the physiological role of which remains unclear. Here, we elucidate the structure-function relationship of this novel epigenetic reader and detail the biological and mechanistic consequences of its interaction with nucleosomes. PZP has a globular architecture and forms a 2:1 stoichiometry complex with the nucleosome, bivalently interacting with histone H3 and DNA. This binding impacts the nucleosome dynamics, shifting the DNA unwrapping/rewrapping equilibrium toward the unwrapped state and increasing DNA accessibility. We demonstrate that the DNA-binding function of the BRPF1 PZP domain is required for the MOZ-BRPF1-ING5-hEaf6 HAT complex to be recruited to chromatin and to acetylate nucleosomal histones. Our findings reveal a novel link between chromatin dynamics and MOZ-mediated acetylation. PubMed: 26626149DOI: 10.1093/nar/gkv1321 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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