5X0X

Complex of Snf2-Nucleosome complex with Snf2 bound to position +6 of the nucleosome

5X0X の概要

• エントリーDOI: 10.2210/pdb5x0x/pdb
• 関連するPDBエントリー: 5X0Y
• EMDBエントリー: 6699 6700
• 分子名称: Histone H3.2, Histone H4, Histone H2A, ... (7 entities in total)
• 機能のキーワード: snf2, nucleosome, chromatin remodeling, structural protein-hydrolase-dna complex, structural protein/hydrolase/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: 298454.63

構造登録者

Li, M.,Liu, X.,Xia, X.,Chen, Z.,Li, X. (登録日: 2017-01-23, 公開日: 2017-04-19, 最終更新日: 2025-07-02)

主引用文献

Liu, X.,Li, M.,Xia, X.,Li, X.,Chen, Z.
Mechanism of chromatin remodelling revealed by the Snf2-nucleosome structure.
Nature, 544:440-445, 2017

PubMed Abstract: Chromatin remodellers are helicase-like, ATP-dependent enzymes that alter chromatin structure and nucleosome positions to allow regulatory proteins access to DNA. Here we report the cryo-electron microscopy structure of chromatin remodeller Switch/sucrose non-fermentable (SWI2/SNF2) from Saccharomyces cerevisiae bound to the nucleosome. The structure shows that the two core domains of Snf2 are realigned upon nucleosome binding, suggesting activation of the enzyme. The core domains contact each other through two induced Brace helices, which are crucial for coupling ATP hydrolysis to chromatin remodelling. Snf2 binds to the phosphate backbones of one DNA gyre of the nucleosome mainly through its helicase motifs within the major domain cleft, suggesting a conserved mechanism of substrate engagement across different remodellers. Snf2 contacts the second DNA gyre via a positively charged surface, providing a mechanism to anchor the remodeller at a fixed position of the nucleosome. Snf2 locally deforms nucleosomal DNA at the site of binding, priming the substrate for the remodelling reaction. Together, these findings provide mechanistic insights into chromatin remodelling.

PubMed: 28424519
DOI: 10.1038/nature22036

実験手法

ELECTRON MICROSCOPY (3.97 Å)