5X0Y

Complex of Snf2-Nucleosome complex with Snf2 bound to SHL2 of the nucleosome

Summary for 5X0Y

• Entry DOI: 10.2210/pdb5x0y/pdb
• Related: 5X0X
• EMDB information: 6699 6700
• Descriptor: Histone H3.2, Histone H4, Histone H2A, ... (7 entities in total)
• Functional Keywords: snf2, nucleosome, chromatin remodeling, structural protein-hydrolase-dna complex, structural protein/hydrolase/dna
• Biological source: Xenopus laevis (African clawed frog); More
• Total number of polymer chains: 11
• Total formula weight: 297020.77

Authors

Li, M.,Liu, X.,Xia, X.,Chen, Z.,Li, X. (deposition date: 2017-01-23, release date: 2017-04-19, Last modification date: 2024-03-27)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (4.69 Å)