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9CAN

S.c INO80 in complex with Xenopus 0/40 nucleosome

This is a non-PDB format compatible entry.
Summary for 9CAN
Entry DOI10.2210/pdb9can/pdb
EMDB information45397
DescriptorHistone H3, RuvB-like protein 1, RuvB-like protein 2, ... (13 entities in total)
Functional Keywordschromatin remodeler, nucleosome, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
Biological sourceXenopus laevis (African clawed frog)
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Total number of polymer chains20
Total formula weight869198.11
Authors
Wu, H.,Kaur, U.,Narlikar, G.J.,Cheng, Y.F. (deposition date: 2024-06-17, 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 (3.3 Å)
Structure validation

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