6TDA
Structure of SWI/SNF chromatin remodeler RSC bound to a nucleosome
Summary for 6TDA
| Entry DOI | 10.2210/pdb6tda/pdb |
| EMDB information | 10465 |
| Descriptor | Histone H3.2, Chromatin structure-remodeling complex subunit RSC9, Chromatin structure-remodeling complex protein RSC6, ... (20 entities in total) |
| Functional Keywords | chromatin remodeler dna binding nucleosome binding atpase transcription, dna binding protein |
| Biological source | Xenopus laevis (African clawed frog) More |
| Total number of polymer chains | 23 |
| Total formula weight | 1054129.14 |
| Authors | Wagner, F.R.,Dienemann, C.,Wang, H.,Stuetzer, A.,Tegunov, D.,Urlaub, H.,Cramer, P. (deposition date: 2019-11-08, release date: 2020-03-18, Last modification date: 2024-11-13) |
| Primary citation | Wagner, F.R.,Dienemann, C.,Wang, H.,Stutzer, A.,Tegunov, D.,Urlaub, H.,Cramer, P. Structure of SWI/SNF chromatin remodeller RSC bound to a nucleosome. Nature, 579:448-451, 2020 Cited by PubMed Abstract: Chromatin-remodelling complexes of the SWI/SNF family function in the formation of nucleosome-depleted, transcriptionally active promoter regions (NDRs). In the yeast Saccharomyces cerevisiae, the essential SWI/SNF complex RSC contains 16 subunits, including the ATP-dependent DNA translocase Sth1. RSC removes nucleosomes from promoter regions and positions the specialized +1 and -1 nucleosomes that flank NDRs. Here we present the cryo-electron microscopy structure of RSC in complex with a nucleosome substrate. The structure reveals that RSC forms five protein modules and suggests key features of the remodelling mechanism. The body module serves as a scaffold for the four flexible modules that we call DNA-interacting, ATPase, arm and actin-related protein (ARP) modules. The DNA-interacting module binds extra-nucleosomal DNA and is involved in the recognition of promoter DNA elements that influence RSC functionality. The ATPase and arm modules sandwich the nucleosome disc with the Snf2 ATP-coupling (SnAC) domain and the finger helix, respectively. The translocase motor of the ATPase module engages with the edge of the nucleosome at superhelical location +2. The mobile ARP module may modulate translocase-nucleosome interactions to regulate RSC activity. The RSC-nucleosome structure provides a basis for understanding NDR formation and the structure and function of human SWI/SNF complexes that are frequently mutated in cancer. PubMed: 32188943DOI: 10.1038/s41586-020-2088-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (15 Å) |
Structure validation
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