8V4Y
Cryo-EM structure of singly-bound SNF2h-nucleosome complex with SNF2h at inactive SHL2 (conformation 1)
Summary for 8V4Y
| Entry DOI | 10.2210/pdb8v4y/pdb |
| Related | 8V6V |
| EMDB information | 42977 43000 43001 43002 |
| Descriptor | Histone H3.2, BERYLLIUM TRIFLUORIDE ION, Histone H4, ... (10 entities in total) |
| Functional Keywords | nucleosome, chromatin remodeler, iswi, snf2h, dna binding protein-dna complex, dna binding protein/dna |
| Biological source | Xenopus laevis (African clawed frog) More |
| Total number of polymer chains | 11 |
| Total formula weight | 358510.40 |
| Authors | Chio, U.S.,Palovcak, E.,Armache, J.P.,Narlikar, G.J.,Cheng, Y. (deposition date: 2023-11-29, release date: 2024-03-20) |
| Primary citation | Chio, U.S.,Palovcak, E.,Smith, A.A.A.,Autzen, H.,Munoz, E.N.,Yu, Z.,Wang, F.,Agard, D.A.,Armache, J.P.,Narlikar, G.J.,Cheng, Y. Functionalized graphene-oxide grids enable high-resolution cryo-EM structures of the SNF2h-nucleosome complex without crosslinking. Nat Commun, 15:2225-2225, 2024 Cited by PubMed Abstract: Single-particle cryo-EM is widely used to determine enzyme-nucleosome complex structures. However, cryo-EM sample preparation remains challenging and inconsistent due to complex denaturation at the air-water interface (AWI). Here, to address this issue, we develop graphene-oxide-coated EM grids functionalized with either single-stranded DNA (ssDNA) or thiol-poly(acrylic acid-co-styrene) (TAASTY) co-polymer. These grids protect complexes between the chromatin remodeler SNF2h and nucleosomes from the AWI and facilitate collection of high-quality micrographs of intact SNF2h-nucleosome complexes in the absence of crosslinking. The data yields maps ranging from 2.3 to 3 Å in resolution. 3D variability analysis reveals nucleotide-state linked conformational changes in SNF2h bound to a nucleosome. In addition, the analysis provides structural evidence for asymmetric coordination between two SNF2h protomers acting on the same nucleosome. We envision these grids will enable similar detailed structural analyses for other enzyme-nucleosome complexes and possibly other protein-nucleic acid complexes in general. PubMed: 38472177DOI: 10.1038/s41467-024-46178-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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