9C9T
S.c INO80 in complex with S.c 0/40 nucleosome, Class 2
This is a non-PDB format compatible entry.
Summary for 9C9T
Entry DOI | 10.2210/pdb9c9t/pdb |
EMDB information | 45370 |
Descriptor | Histone H3, RuvB-like protein 1, RuvB-like protein 2, ... (13 entities in total) |
Functional Keywords | chromatin remodeler, nucleosome, dna binding protein, dna binding protein-dna complex, dna binding protein/dna |
Biological source | Saccharomyces cerevisiae (brewer's yeast) More |
Total number of polymer chains | 20 |
Total formula weight | 870230.31 |
Authors | Wu, H.,Kaur, U.,Narlikar, G.J.,Cheng, Y.F. (deposition date: 2024-06-15, release date: 2025-07-16, Last modification date: 2025-07-30) |
Primary citation | Kaur, 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: 40674492DOI: 10.1126/science.adr3831 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.16 Å) |
Structure validation
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