5X6O

Intact ATR/Mec1-ATRIP/Ddc2 complex

5X6O の概要

• エントリーDOI: 10.2210/pdb5x6o/pdb
• EMDBエントリー: 6708
• 分子名称: Serine/threonine-protein kinase MEC1, DNA damage checkpoint protein LCD1 (2 entities in total)
• 機能のキーワード: atr/mec1, kinase, dimeric, transferase, transferase-dna binding protein complex, transferase/dna binding protein
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 360214.41

構造登録者

Wang, X.,Ran, T.,Cai, G. (登録日: 2017-02-22, 公開日: 2017-12-20, 最終更新日: 2024-10-30)

主引用文献

Wang, X.,Ran, T.,Zhang, X.,Xin, J.,Zhang, Z.,Wu, T.,Wang, W.,Cai, G.
3.9 angstrom structure of the yeast Mec1-Ddc2 complex, a homolog of human ATR-ATRIP.
Science, 358:1206-1209, 2017

PubMed 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.

PubMed: 29191911
DOI: 10.1126/science.aan8414

実験手法

ELECTRON MICROSCOPY (3.9 Å)