6kw4

The ClassB RSC-Nucleosome ComplexThe ClassB RSC-Nucleosome Complex

6kw4, resolution 7.55Å Show:Asymmetric Unit Biological Assembly Structural highlights 6kw4 is a 13 chain structure with sequence from Homo sapiens, Saccharomyces cerevisiae S288C and Xenopus laevis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 7.55Å Ligands: Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H32_XENLA Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Publication Abstract from PubMed The RSC complex remodels chromatin structure and regulates gene transcription. We report the cryoEM structure of yeast RSC bound to the nucleosome. RSC is delineated into the ATPase motor, the actin-related-protein (ARP) module, and the substrate-recruitment module (SRM). RSC binds the nucleosome mainly through the motor, with the auxiliary subunit Sfh1 engaging the H2A-H2B acidic patch to enable nucleosome ejection. SRM is organized into three substrate-binding lobes poised to bind their respective nucleosomal epitopes. The relative orientations of the SRM and the motor on the nucleosome explain the directionality of DNA translocation and promoter nucleosome repositioning by RSC. Together, our findings shed light on RSC assembly and functionality, and provide a framework to understand the mammalian homologs BAF/PBAF and the Sfh1 ortholog INI1/BAF47, which are frequently mutated in cancers. Structure of the RSC complex bound to the nucleosome.,Ye Y, Wu H, Chen K, Clapier CR, Verma N, Zhang W, Deng H, Cairns BR, Gao N, Chen Z Science. 2019 Oct 31. pii: science.aay0033. doi: 10.1126/science.aay0033. PMID:31672915 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Actin-related protein 3D structures Helicase 3D structures Histone 3D structures