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9CCD

DeltaNhp10 INO80 bound to S.c 0/40 nucleosome, INO80 core module

This is a non-PDB format compatible entry.
Summary for 9CCD
Entry DOI10.2210/pdb9ccd/pdb
EMDB information45441
DescriptorChromatin-remodeling ATPase INO80, Actin-related protein 5, Chromatin-remodeling complex subunit IES6, ... (7 entities in total)
Functional Keywordschromatin remodeler, nucleosome, dna binding protein
Biological sourceSaccharomyces cerevisiae (brewer's yeast)
More
Total number of polymer chains10
Total formula weight619884.22
Authors
Wu, H.,Kaur, U.,Narlikar, G.J.,Cheng, Y.F. (deposition date: 2024-06-21, release date: 2025-07-16, Last modification date: 2025-07-30)
Primary citationKaur, U.,Wu, H.,Cheng, Y.,Narlikar, G.J.
Autoinhibition imposed by a large conformational switch of INO80 regulates nucleosome positioning.
Science, 389:eadr3831-eadr3831, 2025
Cited by
PubMed Abstract: Increasing the flanking DNA from 40 to 80 base pairs (bp) causes ~100-fold faster nucleosome sliding by INO80. A prevalent hypothesis posits that the Arp8 module within INO80 enables a ruler-like activity. Using cryogenic electron microscopy, we show that on nucleosomes with 40 bp of flanking DNA, the Arp8 module rotates 180° away from the DNA. Deleting the Arp8 module enables rapid sliding irrespective of flanking DNA length. Thus, rather than enabling a ruler-like activity, the Arp8 module acts as a brake on INO80 remodeling when flanking DNA is short. This autoinhibition-based mechanism has broad implications for understanding how primitive nucleosome mobilization enzymes may have evolved into sophisticated remodelers.
PubMed: 40674492
DOI: 10.1126/science.adr3831
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.01 Å)
Structure validation

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