5B75

Crystal structure of MOZ double PHD finger in complex with histone H3 butyrylation at K14

5B75 の概要

• エントリーDOI: 10.2210/pdb5b75/pdb
• 分子名称: Histone acetyltransferase KAT6A, Histone H3, ZINC ION, ... (5 entities in total)
• 機能のキーワード: moz double phd finger, transferase
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus: Q92794; Chromosome . Nucleus : K7EMV3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 17991.47

構造登録者

Li, H.,Xiong, X. (登録日: 2016-06-05, 公開日: 2016-10-26, 最終更新日: 2023-11-08)

主引用文献

Xiong, X.,Panchenko, T.,Yang, S.,Zhao, S.,Yan, P.,Zhang, W.,Xie, W.,Li, Y.,Zhao, Y.,Allis, C.D.,Li, H.
Selective recognition of histone crotonylation by double PHD fingers of MOZ and DPF2
Nat.Chem.Biol., 12:1111-1118, 2016

PubMed Abstract: Recognition of histone covalent modifications by 'reader' modules constitutes a major mechanism for epigenetic regulation. A recent upsurge of newly discovered histone lysine acylations, such as crotonylation (Kcr), butyrylation (Kbu), and propionylation (Kpr), greatly expands the coding potential of histone lysine modifications. Here we demonstrate that the histone acetylation-binding double PHD finger (DPF) domains of human MOZ (also known as KAT6A) and DPF2 (also known as BAF45d) accommodate a wide range of histone lysine acylations with the strongest preference for Kcr. Crystal structures of the DPF domain of MOZ in complex with H3K14cr, H3K14bu, and H3K14pr peptides reveal that these non-acetyl acylations are anchored in a hydrophobic 'dead-end' pocket with selectivity for crotonylation arising from intimate encapsulation and an amide-sensing hydrogen bonding network. Immunofluorescence and chromatin immunoprecipitation (ChIP)-quantitative PCR (qPCR) showed that MOZ and H3K14cr colocalize in a DPF-dependent manner. Our studies call attention to a new regulatory mechanism centered on histone crotonylation readout by DPF family members.

PubMed: 27775714
DOI: 10.1038/nchembio.2218

実験手法

X-RAY DIFFRACTION (1.704 Å)