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6K15

RSC substrate-recruitment module

Summary for 6K15
Entry DOI10.2210/pdb6k15/pdb
EMDB information9905
DescriptorChromatin structure-remodeling complex subunit RSC7, Chromatin structure-remodeling complex protein RSC3, Chromatin structure-remodeling complex subunit RSC4, ... (13 entities in total)
Functional Keywordschromatin remodeler, swi/snf family, dna binding protein
Biological sourceSaccharomyces cerevisiae S288c (Baker's yeast)
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Total number of polymer chains13
Total formula weight946779.49
Authors
Ye, Y.P.,Wu, H.,Chen, K.J.,Verma, N.,Cairns, B.,Gao, N.,Chen, Z.C. (deposition date: 2019-05-09, release date: 2019-11-13, Last modification date: 2024-03-27)
Primary citationYe, Y.,Wu, H.,Chen, K.,Clapier, C.R.,Verma, N.,Zhang, W.,Deng, H.,Cairns, B.R.,Gao, N.,Chen, Z.
Structure of the RSC complex bound to the nucleosome.
Science, 366:838-843, 2019
Cited by
PubMed Abstract: The RSC complex remodels chromatin structure and regulates gene transcription. We used cryo-electron microscopy to determine the structure of yeast RSC bound to the nucleosome. RSC is delineated into the adenosine triphosphatase motor, the actin-related protein 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. Our findings shed light on RSC assembly and functionality, and they provide a framework to understand the mammalian homologs BAF/PBAF and the Sfh1 ortholog INI1/BAF47, which are frequently mutated in cancers.
PubMed: 31672915
DOI: 10.1126/science.aay0033
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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