7YZP

Hairpin-bound state of the E. coli Mre11-Rad50 (SbcCD) head complex bound to ADP and a DNA hairpin

7YZP の概要

• エントリーDOI: 10.2210/pdb7yzp/pdb
• 関連するPDBエントリー: 7YZO
• EMDBエントリー: 14391 14393
• 分子名称: DNA hairpin (59-MER), Nuclease SbcCD subunit D, Nuclease SbcCD subunit C, ... (6 entities in total)
• 機能のキーワード: abc-type atpase, nuclease, dna repair, dna binding protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 353251.16

構造登録者

Gut, F.,Kaeshammer, L.,Lammens, K.,Bartho, J.,van de Logt, E.,Kessler, B.,Hopfner, K.P. (登録日: 2022-02-21, 公開日: 2022-08-17, 最終更新日: 2025-07-02)

主引用文献

Gut, F.,Kashammer, L.,Lammens, K.,Bartho, J.D.,Boggusch, A.M.,van de Logt, E.,Kessler, B.,Hopfner, K.P.
Structural mechanism of endonucleolytic processing of blocked DNA ends and hairpins by Mre11-Rad50.
Mol.Cell, 82:3513-3522.e6, 2022

PubMed Abstract: DNA double-strand breaks (DSBs) threaten genome stability and are linked to tumorigenesis in humans. Repair of DSBs requires the removal of attached proteins and hairpins through a poorly understood but physiologically critical endonuclease activity by the Mre11-Rad50 complex. Here, we report cryoelectron microscopy (cryo-EM) structures of the bacterial Mre11-Rad50 homolog SbcCD bound to a protein-blocked DNA end and a DNA hairpin. The structures reveal that Mre11-Rad50 bends internal DNA for endonucleolytic cleavage and show how internal DNA, DNA ends, and hairpins are processed through a similar ATP-regulated conformational state. Furthermore, Mre11-Rad50 is loaded onto blocked DNA ends with Mre11 pointing away from the block, explaining the distinct biochemistries of 3' → 5' exonucleolytic and endonucleolytic incision through the way Mre11-Rad50 interacts with diverse DNA ends. In summary, our results unify Mre11-Rad50's enigmatic nuclease diversity within a single structural framework and reveal how blocked DNA ends and hairpins are processed.

PubMed: 35987200
DOI: 10.1016/j.molcel.2022.07.019

実験手法

ELECTRON MICROSCOPY (4 Å)