5GK9

Crystal structure of human HBO1 in complex with BRPF2

5GK9 の概要

• エントリーDOI: 10.2210/pdb5gk9/pdb
• 分子名称: Histone acetyltransferase KAT7, BRD1 protein, ZINC ION, ... (5 entities in total)
• 機能のキーワード: hat, transferase-metal binding protein complex, transferase/metal binding protein
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus, nucleoplasm : O95251
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39130.24

構造登録者

Tao, Y.,Zhu, J.,Xu, S.,Ding, J. (登録日: 2016-07-04, 公開日: 2017-03-29, 最終更新日: 2023-11-08)

主引用文献

Tao, Y.,Zhong, C.,Zhu, J.,Xu, S.,Ding, J.
Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2.
Nucleic Acids Res., 45:5707-5719, 2017

PubMed Abstract: HBO1, a member of the MYST family of histone acetyltransferases (HATs), is required for global acetylation of histone H3K14 and embryonic development. It functions as a catalytic subunit in multisubunit complexes comprising a BRPF1/2/3 or JADE1/2/3 scaffold protein, and two accessory proteins. BRPF2 has been shown to be important for the HAT activity of HBO1 toward H3K14. Here we demonstrated that BRPF2 can regulate the HAT activity of HBO1 toward free H3 and H4, and nucleosomal H3. Particularly, a short N-terminal region of BRPF2 is sufficient for binding to HBO1 and can potentiate its activity toward H3K14. The crystal structure of the HBO1 MYST domain in complex with this segment of BRPF2 together with the biochemical and cell biological data revealed the key residues responsible for the HBO1-BRPF2 interaction. Our structural and functional data together indicate that the N-terminal region of BRPF2 plays an important role in the binding of HBO1 and a minor role in the binding of nucleosomes, which provide new mechanistic insights into the regulation of the HAT activity of HBO1 by BRPF2.

PubMed: 28334966
DOI: 10.1093/nar/gkx142

実験手法

X-RAY DIFFRACTION (2.4 Å)