7XAY

Crystal structure of Hat1-Hat2-Asf1-H3-H4

7XAY の概要

• エントリーDOI: 10.2210/pdb7xay/pdb
• 分子名称: Soluble cytochrome b562,Histone acetyltransferase type B catalytic subunit, Histone acetyltransferase type B subunit 2, Histone chaperone asf1, ... (6 entities in total)
• 機能のキーワード: histone acetyltransferase, histones, enzymatic activity, histone chaperone, transferase
• 由来する生物種: Saccharomyces cerevisiae S288C; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 137609.16

構造登録者

Yue, Y.,Yang, W.S.,Xu, R.M. (登録日: 2022-03-19, 公開日: 2022-05-18, 最終更新日: 2023-11-29)

主引用文献

Yue, Y.,Yang, W.S.,Zhang, L.,Liu, C.P.,Xu, R.M.
Topography of histone H3-H4 interaction with the Hat1-Hat2 acetyltransferase complex.
Genes Dev., 36:408-413, 2022

PubMed Abstract: Chaperones influence histone conformation and intermolecular interaction in multiprotein complexes, and the structures obtained with full-length histones often provide more accurate and comprehensive views. Here, our structure of the Hat1-Hat2 acetyltransferase complex bound to Asf1-H3-H4 shows that the core domains of H3 and H4 are involved in binding Hat1 and Hat2, and the N-terminal tail of H3 makes extensive interaction with Hat2. These findings expand the knowledge about histone-protein interaction and implicate a function of Hat2/RbAp46/48, which is a versatile histone chaperone found in many chromatin-associated complexes, in the passing of histones between chaperones.

PubMed: 35393344
DOI: 10.1101/gad.349099.121

実験手法

X-RAY DIFFRACTION (3.3 Å)