8EUF

Class2 of the INO80-Nucleosome complex

This is a non-PDB format compatible entry.

Summary for 8EUF

• Entry DOI: 10.2210/pdb8euf/pdb
• EMDB information: 28613
• Descriptor: Chromatin-remodeling ATPase INO80, Actin-related protein 5, Chromatin-remodeling complex subunit IES6, ... (7 entities in total)
• Functional Keywords: chromatin remodeler, hexasome, dna binding protein, dna binding protein-hydrolase complex, dna binding protein/hydrolase
• Biological source: Saccharomyces cerevisiae S288C; More
• Total number of polymer chains: 10
• Total formula weight: 619884.22

Authors

Wu, H.,Munoz, E.,Gourdet, M.,Narlikar, G.,Cheng, Y.F. (deposition date: 2022-10-18, release date: 2023-07-12, Last modification date: 2023-08-16)

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

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: 37384669
DOI: 10.1126/science.adf4197

Experimental method

ELECTRON MICROSCOPY (3.41 Å)