Summary for 8QZ0
| Entry DOI | 10.2210/pdb8qz0/pdb |
| EMDB information | 18769 |
| Descriptor | Histone H3, Actin-like protein ARP6, Vacuolar protein sorting-associated protein 71, ... (20 entities in total) |
| Functional Keywords | chromatin remodelling complex, hexasome-dimer complex, dna binding protein |
| Biological source | Saccharomyces cerevisiae S288C More |
| Total number of polymer chains | 22 |
| Total formula weight | 893304.36 |
| Authors | Jalal, A.S.B.,Wigley, D.B. (deposition date: 2023-10-26, release date: 2024-10-02, Last modification date: 2024-10-30) |
| Primary citation | Jalal, A.S.B.,Girvan, P.,Chua, E.Y.D.,Liu, L.,Wang, S.,McCormack, E.A.,Skehan, M.T.,Knight, C.L.,Rueda, D.S.,Wigley, D.B. Stabilization of the hexasome intermediate during histone exchange by yeast SWR1 complex. Mol.Cell, 84:3871-, 2024 Cited by PubMed Abstract: The yeast SWR1 complex catalyzes the exchange of histone H2A/H2B dimers in nucleosomes with Htz1/H2B dimers. We use cryoelectron microscopy to determine the structure of an enzyme-bound hexasome intermediate in the reaction pathway of histone exchange, in which an H2A/H2B dimer has been extracted from a nucleosome prior to the insertion of a dimer comprising Htz1/H2B. The structure reveals a key role for the Swc5 subunit in stabilizing the unwrapping of DNA from the histone core of the hexasome. By engineering a crosslink between an Htz1/H2B dimer and its chaperone protein Chz1, we show that this blocks histone exchange by SWR1 but allows the incoming chaperone-dimer complex to insert into the hexasome. We use this reagent to trap an SWR1/hexasome complex with an incoming Htz1/H2B dimer that shows how the reaction progresses to the next step. Taken together the structures reveal insights into the mechanism of histone exchange by SWR1 complex. PubMed: 39226902DOI: 10.1016/j.molcel.2024.08.015 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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