8OO7

CryoEM Structure INO80core Hexasome complex composite model state1

This is a non-PDB format compatible entry.

Summary for 8OO7

• Entry DOI: 10.2210/pdb8oo7/pdb
• Related: 8OO9 8OOA 8OOC 8OOF 8OOK
• EMDB information: 17006 17007 17008 17010 17012 17017 17019 17023
• Descriptor: RuvB-like protein 1, Histone H4, Histone H2A, ... (16 entities in total)
• Functional Keywords: atp-dependent chromatin remodeler, dna binding protein
• Biological source: Thermochaetoides thermophila; More
• Total number of polymer chains: 18
• Total formula weight: 830296.70

Authors

Zhang, M.,Jungblut, A.,Hoffmann, T.,Eustermann, S. (deposition date: 2023-04-04, release date: 2023-07-26, Last modification date: 2024-07-24)

Primary citation

Zhang, M.,Jungblut, A.,Kunert, F.,Hauptmann, L.,Hoffmann, T.,Kolesnikova, O.,Metzner, F.,Moldt, M.,Weis, F.,DiMaio, F.,Hopfner, K.P.,Eustermann, S.
Hexasome-INO80 complex reveals structural basis of noncanonical nucleosome remodeling.
Science, 381:313-319, 2023

PubMed Abstract: Loss of H2A-H2B histone dimers is a hallmark of actively transcribed genes, but how the cellular machinery functions in the context of noncanonical nucleosomal particles remains largely elusive. In this work, we report the structural mechanism for adenosine 5'-triphosphate-dependent chromatin remodeling of hexasomes by the INO80 complex. We show how INO80 recognizes noncanonical DNA and histone features of hexasomes that emerge from the loss of H2A-H2B. A large structural rearrangement switches the catalytic core of INO80 into a distinct, spin-rotated mode of remodeling while its nuclear actin module remains tethered to long stretches of unwrapped linker DNA. Direct sensing of an exposed H3-H4 histone interface activates INO80, independently of the H2A-H2B acidic patch. Our findings reveal how the loss of H2A-H2B grants remodelers access to a different, yet unexplored layer of energy-driven chromatin regulation.

PubMed: 37384673
DOI: 10.1126/science.adf6287

Experimental method

ELECTRON MICROSCOPY (2.8 Å)