9NH8

CHD1-nucleosome complex (anchored state)

9NH8 の概要

• エントリーDOI: 10.2210/pdb9nh8/pdb
• EMDBエントリー: 42693 49406
• 分子名称: Histone H3.2, Histone H4, Histone H2A, ... (8 entities in total)
• 機能のキーワード: chromatin, remodeler, genome organization, nuclear protein, nuclear protein-dna complex, nuclear protein/dna
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 403252.77

構造登録者

James, A.M.,Farnung, L. (登録日: 2025-02-24, 公開日: 2025-05-07, 最終更新日: 2025-05-28)

主引用文献

James, A.M.,Farnung, L.
Structural basis of human CHD1 nucleosome recruitment and pausing.
Mol.Cell, 85:1938-1951.e6, 2025

PubMed Abstract: Chromatin remodelers regulate gene expression and genome maintenance by controlling nucleosome positioning, but the structural basis for their regulated and directional activity remains poorly understood. Here, we present three cryoelectron microscopy (cryo-EM) structures of human chromodomain helicase DNA-binding protein 1 (CHD1) bound to nucleosomes that reveal previously unobserved recruitment and regulatory states. We identify a structural element, termed the "anchor element," that connects the CHD1 ATPase motor to the nucleosome entry-side acidic patch. The anchor element coordinates with other regulatory modules, including the gating element, which undergoes a conformational switch critical for remodeling. Our structures demonstrate how the DNA-binding region of CHD1 binds entry- and exit-side DNA during remodeling to achieve directional sliding. The observed structural elements are conserved across chromatin remodelers, suggesting a unified mechanism for nucleosome recognition and remodeling. Our findings show how chromatin remodelers couple nucleosome recruitment to regulated DNA translocation, providing a framework for understanding chromatin remodeler mechanisms beyond DNA translocation.

PubMed: 40334658
DOI: 10.1016/j.molcel.2025.04.020

実験手法

ELECTRON MICROSCOPY (3.2 Å)