9CB7
DeltaNhp10 INO80 bound to S.c 0/40 nucleosome, Ino80-Nucleosome
This is a non-PDB format compatible entry.
Summary for 9CB7
| Entry DOI | 10.2210/pdb9cb7/pdb |
| EMDB information | 45418 |
| Descriptor | Histone H3, Histone H4, Histone H2A.1, ... (8 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 | 12 |
| Total formula weight | 458250.86 |
| Authors | Wu, H.,Kaur, U.,Narlikar, G.J.,Cheng, Y.F. (deposition date: 2024-06-18, 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 (4.04 Å) |
Structure validation
Download full validation report
