EMD-0968

Single-particle
3.0 Å
EMD-0968 Deposition: 21/01/2020
Map released: 12/02/2020
Last modified: 11/08/2021
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-0968

Structure of human BAF Base module

EMD-0968

Single-particle
3.0 Å
EMD-0968 Deposition: 21/01/2020
Map released: 12/02/2020
Last modified: 11/08/2021
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Homo sapiens
Sample: Structure of nucleosome-bound human BAF Base module
Fitted models: 6lth (Avg. Q-score: 0.526)

Deposition Authors: Shuang H, Zihan W, Yuan T, Zishuo Y, Jiali Y, Xinxin W, Jie L, Bijun L, Yanhui X
Structure of nucleosome-bound human BAF complex.
He S , Wu Z, Tian Y , Yu Z, Yu J , Wang X, Li J, Liu B , Xu Y
(2020) Science , 367 , 875 - 881
PUBMED: 32001526
DOI: doi:10.1126/science.aaz9761
ISSN: 1095-9203
ASTM: SCIEAS
Abstract:
Mammalian SWI/SNF family chromatin remodelers, BRG1/BRM-associated factor (BAF) and polybromo-associated BAF (PBAF), regulate chromatin structure and transcription, and their mutations are linked to cancers. The 3.7-angstrom-resolution cryo-electron microscopy structure of human BAF bound to the nucleosome reveals that the nucleosome is sandwiched by the base and the adenosine triphosphatase (ATPase) modules, which are bridged by the actin-related protein (ARP) module. The ATPase motor is positioned proximal to nucleosomal DNA and, upon ATP hydrolysis, engages with and pumps DNA along the nucleosome. The C-terminal α helix of SMARCB1, enriched in positively charged residues frequently mutated in cancers, mediates interactions with an acidic patch of the nucleosome. AT-rich interactive domain-containing protein 1A (ARID1A) and the SWI/SNF complex subunit SMARCC serve as a structural core and scaffold in the base module organization, respectively. Our study provides structural insights into subunit organization and nucleosome recognition of human BAF complex.