EMD-6708

Single-particle
3.9 Å
EMD-6708 Deposition: 22/02/2017
Map released: 20/12/2017
Last modified: 30/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-6708

Intact ATR/Mec1-ATRIP/Ddc2 complex

EMD-6708

Single-particle
3.9 Å
EMD-6708 Deposition: 22/02/2017
Map released: 20/12/2017
Last modified: 30/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Saccharomyces cerevisiae
Sample: ATR/Mec1-ATRIP/Ddc2
Fitted models: 5x6o (Avg. Q-score: 0.41)

Deposition Authors: Wang X , Ran T
3.9 angstrom structure of the yeast Mec1-Ddc2 complex, a homolog of human ATR-ATRIP.
Wang X , Ran T , Zhang X, Xin J, Zhang Z, Wu T, Wang W , Cai G
(2017) Science , 358 , 1206 - 1209
PUBMED: 29191911
DOI: doi:10.1126/science.aan8414
ISSN: 1095-9203
ASTM: SCIEAS
Abstract:
The ataxia telangiectasia-mutated and Rad3-related (ATR) kinase is a master regulator of DNA damage response and replication stress in humans, but the mechanism of its activation remains unclear. ATR acts together with its partner ATRIP. Using cryo-electron microscopy, we determined the structure of intact Mec1-Ddc2 (the yeast homolog of ATR-ATRIP), which is poised for catalysis, at a resolution of 3.9 angstroms. Mec1-Ddc2 forms a dimer of heterodimers through the PRD and FAT domains of Mec1 and the coiled-coil domain of Ddc2. The PRD and Bridge domains in Mec1 constitute critical regulatory sites. The activation loop of Mec1 is inhibited by the PRD, revealing an allosteric mechanism of kinase activation. Our study clarifies the architecture of ATR-ATRIP and provides a structural framework for the understanding of ATR regulation.