7W9V
Cryo-EM structure of nucleosome in complex with p300 acetyltransferase catalytic core (complex I)
Summary for 7W9V
| Entry DOI | 10.2210/pdb7w9v/pdb |
| EMDB information | 32373 |
| Descriptor | Histone H3.1, Histone H4, Histone H2A type 1-B/E, ... (7 entities in total) |
| Functional Keywords | p300, nucleosome, acetyltransferase, gene regulation |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 11 |
| Total formula weight | 275234.64 |
| Authors | Hatazawa, S.,Liu, J.,Takizawa, Y.,Zandian, M.,Negishi, L.,Kutateladze, T.G.,Kurumizaka, H. (deposition date: 2021-12-10, release date: 2022-07-13, Last modification date: 2024-10-23) |
| Primary citation | Hatazawa, S.,Liu, J.,Takizawa, Y.,Zandian, M.,Negishi, L.,Kutateladze, T.G.,Kurumizaka, H. Structural basis for binding diversity of acetyltransferase p300 to the nucleosome. Iscience, 25:104563-104563, 2022 Cited by PubMed Abstract: p300 is a human acetyltransferase that associates with chromatin and mediates vital cellular processes. We now report the cryo-electron microscopy structures of the p300 catalytic core in complex with the nucleosome core particle (NCP). In the most resolved structure, the HAT domain and bromodomain of p300 contact nucleosomal DNA at superhelical locations 2 and 3, and the catalytic site of the HAT domain are positioned near the N-terminal tail of histone H4. Mutations of the p300-DNA interfacial residues of p300 substantially decrease binding to NCP. Three additional classes of p300-NCP complexes show different modes of the p300-NCP complex formation. Our data provide structural details critical to our understanding of the mechanism by which p300 acetylates multiple sites on the nucleosome. PubMed: 35754730DOI: 10.1016/j.isci.2022.104563 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.95 Å) |
Structure validation
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