6U04

Crystal structure of human BRPF1 PZP bound to histone H3 tail

6U04 の概要

• エントリーDOI: 10.2210/pdb6u04/pdb
• 分子名称: Histone H3.3,BRPF1, Peregrin, PRASEODYMIUM ION, ZINC ION, ... (4 entities in total)
• 機能のキーワード: epigenetics, nucleosome, dna binding, transcription
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22534.18

構造登録者

Klein, B.J.,Kutateladze, T.G. (登録日: 2019-08-13, 公開日: 2019-11-27, 最終更新日: 2023-10-11)

主引用文献

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

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: 31711755
DOI: 10.1016/j.str.2019.10.014

実験手法

X-RAY DIFFRACTION (2.2 Å)