30GF
Structural characterisation of chromatin remodelling intermediates supports linker DNA dependent product inhibition as a mechanism for nucleosome spacing.
Summary for 30GF
| Entry DOI | 10.2210/pdb30gf/pdb |
| EMDB information | 53597 |
| Descriptor | Histone H3.2, Histone H4, Histone H2A, ... (6 entities in total) |
| Functional Keywords | nucleosome, remodelling enzyme, gene regulation |
| Biological source | Saccharomyces cerevisiae More |
| Total number of polymer chains | 10 |
| Total formula weight | 210150.17 |
| Authors | Sundaramoorthy, R.,Hughes, A.,Owen-hughes, T.A. (deposition date: 2026-04-23, release date: 2026-08-26) |
| Primary citation | Hughes, A.L.,Sundaramoorthy, R.,Owen-Hughes, T. Structural characterisation of chromatin remodelling intermediates supports linker DNA-dependent product inhibition as a mechanism for nucleosome spacing. Elife, 14:-, 2025 Cited by PubMed Abstract: Previously we showed that Chd1 chromatin remodelling enzyme associates with nucleosomes oriented towards the longer linker (Sundaramoorthy et al., 2018) (1). Here we report a series of structures of Chd1 bound to nucleosomes during ongoing ATP-dependent repositioning. Combining these with biochemical experiments and existing literature we propose a model in which Chd1 first associates oriented to sample putative entry DNA. In an ATP-dependent reaction, the enzyme then redistributes to the opposite side of the nucleosome, where it subsequently adopts a conformation productive for DNA translocation. Once this active complex extends nascent exit linker to approximately 15bp, it is sensed by the Chd1 DNA binding domain resulting in conversion to a product inhibited state. These observations provide a mechanistic basis for the action of a molecular ruler element in nucleosome spacing. PubMed: 41439750DOI: 10.1038/nsmb1071 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.8 Å) |
Structure validation
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