7W9V

Cryo-EM structure of nucleosome in complex with p300 acetyltransferase catalytic core (complex I)

7W9V の概要

• エントリーDOI: 10.2210/pdb7w9v/pdb
• EMDBエントリー: 32373
• 分子名称: Histone H3.1, Histone H4, Histone H2A type 1-B/E, ... (7 entities in total)
• 機能のキーワード: p300, nucleosome, acetyltransferase, gene regulation
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 275234.64

構造登録者

Hatazawa, S.,Liu, J.,Takizawa, Y.,Zandian, M.,Negishi, L.,Kutateladze, T.G.,Kurumizaka, H. (登録日: 2021-12-10, 公開日: 2022-07-13, 最終更新日: 2024-10-23)

主引用文献

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

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: 35754730
DOI: 10.1016/j.isci.2022.104563

実験手法

ELECTRON MICROSCOPY (3.95 Å)