5W1R

Cryo-EM structure of DNAPKcs

5W1R の概要

• エントリーDOI: 10.2210/pdb5w1r/pdb
• EMDBエントリー: 8751 8752
• 分子名称: DNA-dependent protein kinase catalytic subunit (1 entity in total)
• 機能のキーワード: dnap, pikk, nhej, v(d)j recombination, dna binding protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 469673.22

構造登録者

Sharif, H.,Li, Y.,Wu, H. (登録日: 2017-06-04, 公開日: 2017-07-19, 最終更新日: 2025-05-21)

主引用文献

Sharif, H.,Li, Y.,Dong, Y.,Dong, L.,Wang, W.L.,Mao, Y.,Wu, H.
Cryo-EM structure of the DNA-PK holoenzyme.
Proc. Natl. Acad. Sci. U.S.A., 114:7367-7372, 2017

PubMed Abstract: DNA-dependent protein kinase (DNA-PK) is a large protein complex central to the nonhomologous end joining (NHEJ) DNA-repair pathway. It comprises the DNA-PK catalytic subunit (DNA-PKcs) and the heterodimer of DNA-binding proteins Ku70 and Ku80. Here, we report the cryo-electron microscopy (cryo-EM) structures of human DNA-PKcs at 4.4-Å resolution and the DNA-PK holoenzyme at 5.8-Å resolution. The DNA-PKcs structure contains three distinct segments: the N-terminal region with an arm and a bridge, the circular cradle, and the head that includes the kinase domain. Two perpendicular apertures exist in the structure, which are sufficiently large for the passage of dsDNA. The DNA-PK holoenzyme cryo-EM map reveals density for the C-terminal globular domain of Ku80 that interacts with the arm of DNA-PKcs. The Ku80-binding site is adjacent to the previously identified density for the DNA-binding region of the Ku70/Ku80 complex, suggesting concerted DNA interaction by DNA-PKcs and the Ku complex.

PubMed: 28652322
DOI: 10.1073/pnas.1707386114

実験手法

ELECTRON MICROSCOPY (4.4 Å)