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Title3.9 Å structure of the yeast Mec1-Ddc2 complex, a homolog of human ATR-ATRIP.
Journal, issue, pagesScience, Vol. 358, Issue 6367, Page 1206-1209, Year 2017
Publish dateDec 1, 2017
AuthorsXuejuan Wang / Tingting Ran / Xuan Zhang / Jiyu Xin / Zhihui Zhang / Tengwei Wu / Weiwu Wang / Gang Cai /
PubMed AbstractThe 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 ...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.
External linksScience / PubMed:29191911
MethodsEM (single particle)
Resolution3.9 Å
Structure data

6708

5x6o

EMDB-6708, PDB-5x6o:
Intact ATR/Mec1-ATRIP/Ddc2 complex
Method: EM (single particle) / Resolution: 3.9 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsTRANSFERASE/DNA BINDING PROTEIN / ATR/Mec1 / Kinase / Dimeric / TRANSFERASE / TRANSFERASE-DNA BINDING PROTEIN complex

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