7X3X

Cryo-EM structure of N1 nucleosome-RA

7X3X の概要

• エントリーDOI: 10.2210/pdb7x3x/pdb
• EMDBエントリー: 32996
• 分子名称: Histone H3, Histone H4, Histone H2A, ... (7 entities in total)
• 機能のキーワード: protein binding-dna complex, protein binding/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: 11
• 化学式量合計: 323530.80

構造登録者

Lifei, L.,Kangjing, C.,Chen, Z. (登録日: 2022-03-01, 公開日: 2023-09-20, 最終更新日: 2025-06-25)

主引用文献

Li, L.,Chen, K.,Sia, Y.,Hu, P.,Ye, Y.,Chen, Z.
Structure of the ISW1a complex bound to the dinucleosome.
Nat.Struct.Mol.Biol., 31:266-274, 2024

PubMed Abstract: Nucleosomes are basic repeating units of chromatin and form regularly spaced arrays in cells. Chromatin remodelers alter the positions of nucleosomes and are vital in regulating chromatin organization and gene expression. Here we report the cryo-EM structure of chromatin remodeler ISW1a complex from Saccharomyces cerevisiae bound to the dinucleosome. Each subunit of the complex recognizes a different nucleosome. The motor subunit binds to the mobile nucleosome and recognizes the acidic patch through two arginine residues, while the DNA-binding module interacts with the entry DNA at the nucleosome edge. This nucleosome-binding mode provides the structural basis for linker DNA sensing of the motor. Notably, the Ioc3 subunit recognizes the disk face of the adjacent nucleosome through interacting with the H4 tail, the acidic patch and the nucleosomal DNA, which plays a role in the spacing activity in vitro and in nucleosome organization and cell fitness in vivo. Together, these findings support the nucleosome spacing activity of ISW1a and add a new mode of nucleosome remodeling in the context of a chromatin environment.

PubMed: 38177688
DOI: 10.1038/s41594-023-01174-6

実験手法

ELECTRON MICROSCOPY (3.2 Å)