6IRO

the crosslinked complex of ISWI-nucleosome in the ADP-bound state

Summary for 6IRO

• Entry DOI: 10.2210/pdb6iro/pdb
• EMDB information: 9718 9719 9720
• Descriptor: ISWI chromatin-remodeling complex ATPase ISW1, Histone H3, Histone H4, ... (8 entities in total)
• Functional Keywords: chromatin remodelling, single particle cryo-em, nucleosome, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 11
• Total formula weight: 334858.82

Authors

Yan, L.J.,Wu, H.,Li, X.M.,Gao, N.,Chen, Z.C. (deposition date: 2018-11-13, release date: 2019-04-03, Last modification date: 2024-03-27)

Primary citation

Yan, L.,Wu, H.,Li, X.,Gao, N.,Chen, Z.
Structures of the ISWI-nucleosome complex reveal a conserved mechanism of chromatin remodeling.
Nat. Struct. Mol. Biol., 26:258-266, 2019

PubMed Abstract: Chromatin remodelers are diverse enzymes, and different models have been proposed to explain how these proteins work. Here we report the 3.3 Å-resolution cryogenic electron microscopy (cryo-EM) structures of Saccharomyces cerevisiae ISWI (ISW1) in complex with the nucleosome in adenosine diphosphate (ADP)-bound and ADP-BeF-bound states. The data show that after nucleosome binding, ISW1 is activated by substantial rearrangement of the catalytic domains, with the regulatory AutoN domain packing the first RecA-like core and the NegC domain being disordered. The high-resolution structure reveals local DNA distortion and translocation induced by ISW1 in the ADP-bound state, which is essentially identical to that induced by the Snf2 chromatin remodeler, suggesting a common mechanism of DNA translocation. The histone core remains largely unperturbed, and prevention of histone distortion by crosslinking did not inhibit the activity of yeast ISW1 or its human homolog. Together, our findings suggest a general mechanism of chromatin remodeling involving local DNA distortion without notable histone deformation.

PubMed: 30872815
DOI: 10.1038/s41594-019-0199-9

Experimental method

ELECTRON MICROSCOPY (3.4 Å)