7MBM

Cryo-EM structure of MLL1-NCP (H3K4M) complex, mode01

7MBM の概要

• エントリーDOI: 10.2210/pdb7mbm/pdb
• EMDBエントリー: 23738
• 分子名称: Retinoblastoma-binding protein 5, DNA (145-MER), WD repeat-containing protein 5, ... (10 entities in total)
• 機能のキーワード: mll1-ncp, h3k4 methylation, transferase, transferase-dna binding protein-dna complex, transferase/dna binding protein/dna
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 377637.05

構造登録者

Park, S.H.,Ayoub, A.,Lee, Y.T.,Dou, Y.,Cho, U. (登録日: 2021-04-01, 公開日: 2021-12-29, 最終更新日: 2025-05-28)

主引用文献

Ayoub, A.,Park, S.H.,Lee, Y.T.,Cho, U.S.,Dou, Y.
Regulation of MLL1 Methyltransferase Activity in Two Distinct Nucleosome Binding Modes.
Biochemistry, 61:1-9, 2022

PubMed Abstract: Cryo-EM structures of the KMT2A/MLL1 core complex bound on nucleosome core particles (NCPs) suggest unusual rotational dynamics of the MLL1 complex approaching its physiological substrate. However, the functional implication of such dynamics remains unclear. Here, we show that the MLL1 core complex also shows high rotational dynamics bound on the NCP carrying the catalytically inert histone H3 lysine 4 to methionine (K4M) mutation. There are two major binding modes of the MLL1 complex on the NCP. Importantly, disruption of only one of the binding modes compromised the overall MLL1 activity in an NCP-specific manner. We propose that the MLL1 core complex probably exists in an equilibrium of poised and active binding modes. The high rotational dynamics of the MLL1 complex on the NCP is a feature that can be exploited for loci-specific regulation of H3K4 methylation in higher eukaryotes.

PubMed: 34928138
DOI: 10.1021/acs.biochem.1c00603

実験手法

ELECTRON MICROSCOPY (4.76 Å)