Summary for 8ETU
| Entry DOI | 10.2210/pdb8etu/pdb |
| EMDB information | 28599 |
| Descriptor | Actin-related protein 5, Chromatin-remodeling complex subunit IES6, RuvB-like protein 1, ... (7 entities in total) |
| Functional Keywords | chromatin remodeler, hexasome, dna binding protein |
| Biological source | Saccharomyces cerevisiae S288C (baker's yeast) More |
| Total number of polymer chains | 10 |
| Total formula weight | 459576.76 |
| Authors | Wu, H.,Munoz, E.,Gourdet, M.,Cheng, Y.F.,Narlikar, G. (deposition date: 2022-10-17, release date: 2023-07-19, Last modification date: 2024-06-19) |
| Primary citation | Wu, H.,Munoz, E.N.,Hsieh, L.J.,Chio, U.S.,Gourdet, M.A.,Narlikar, G.J.,Cheng, Y. Reorientation of INO80 on hexasomes reveals basis for mechanistic versatility. Science, 381:319-324, 2023 Cited by PubMed Abstract: Unlike other chromatin remodelers, INO80 preferentially mobilizes hexasomes, which can form during transcription. Why INO80 prefers hexasomes over nucleosomes remains unclear. Here, we report structures of INO80 bound to a hexasome or a nucleosome. INO80 binds the two substrates in substantially different orientations. On a hexasome, INO80 places its ATPase subunit, Ino80, at superhelical location -2 (SHL -2), in contrast to SHL -6 and SHL -7, as previously seen on nucleosomes. Our results suggest that INO80 action on hexasomes resembles action by other remodelers on nucleosomes such that Ino80 is maximally active near SHL -2. The SHL -2 position also plays a critical role for nucleosome remodeling by INO80. Overall, the mechanistic adaptations used by INO80 for preferential hexasome sliding imply that subnucleosomal particles play considerable regulatory roles. PubMed: 37384669DOI: 10.1126/science.adf4197 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
Download full validation report
