8OOC
CryoEM Structure INO80core Hexasome complex Rvb core refinement state1
This is a non-PDB format compatible entry.
Summary for 8OOC
| Entry DOI | 10.2210/pdb8ooc/pdb |
| EMDB information | 17006 17010 17012 17019 |
| Descriptor | RuvB-like helicase, Chromatin-remodeling ATPase Ino80, INO80 complex subunit B-like conserved region domain-containing protein, ... (9 entities in total) |
| Functional Keywords | atp-dependent chromatin remodeler, dna binding protein |
| Biological source | Thermochaetoides thermophila More |
| Total number of polymer chains | 10 |
| Total formula weight | 609222.72 |
| Authors | Zhang, M.,Jungblut, A.,Hoffmann, T.,Eustermann, S. (deposition date: 2023-04-05, release date: 2023-08-02, 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 Cited by 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: 37384673DOI: 10.1126/science.adf6287 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.93 Å) |
Structure validation
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