6DS6
Crystal structure of p300 ZZ domain in complex with histone H3 peptide
Summary for 6DS6
| Entry DOI | 10.2210/pdb6ds6/pdb |
| Descriptor | Histone H3 peptide-Histone acetyltransferase p300 Chimeric protein, ZINC ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | p300, zz domain, histone, chromatin, gene regulation, transferase |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 1 |
| Total formula weight | 7012.01 |
| Authors | Zhang, Y.,Kutateladze, T.G. (deposition date: 2018-06-13, release date: 2018-08-29, Last modification date: 2024-03-13) |
| Primary citation | Zhang, Y.,Xue, Y.,Shi, J.,Ahn, J.,Mi, W.,Ali, M.,Wang, X.,Klein, B.J.,Wen, H.,Li, W.,Shi, X.,Kutateladze, T.G. The ZZ domain of p300 mediates specificity of the adjacent HAT domain for histone H3. Nat. Struct. Mol. Biol., 25:841-849, 2018 Cited by PubMed Abstract: Human p300 is a transcriptional co-activator and a major acetyltransferase that acetylates histones and other proteins facilitating gene transcription. The activity of p300 relies on the fine-tuned interactome that involves a dozen p300 domains and hundreds of binding partners and links p300 to a wide range of vital signaling events. Here, we report a novel function of the ZZ-type zinc finger (ZZ) of p300 as a reader of histone H3. We show that the ZZ domain and acetyllysine-recognizing bromodomain of p300 play critical roles in modulating p300 enzymatic activity and its association with chromatin. The acetyllysine binding function of bromodomain is essential for acetylation of histones H3 and H4, whereas interaction of the ZZ domain with H3 promotes selective acetylation of the histone H3K27 and H3K18 sites. PubMed: 30150647DOI: 10.1038/s41594-018-0114-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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