7YOX

Cryo-EM structure of the N-terminal domain of hMCM8/9 and HROB

これはPDB形式変換不可エントリーです。

7YOX の概要

• エントリーDOI: 10.2210/pdb7yox/pdb
• EMDBエントリー: 33989
• 分子名称: DNA helicase MCM8, DNA helicase MCM9 (2 entities in total)
• 機能のキーワード: mcm8/9, hydrolase
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 201163.50

構造登録者

Zheng, J.F.,Weng, Z.F.,Liu, Y.F. (登録日: 2022-08-02, 公開日: 2023-08-09, 最終更新日: 2024-11-13)

主引用文献

Weng, Z.,Zheng, J.,Zhou, Y.,Lu, Z.,Wu, Y.,Xu, D.,Li, H.,Liang, H.,Liu, Y.
Structural and mechanistic insights into the MCM8/9 helicase complex.
Elife, 12:-, 2023

PubMed Abstract: MCM8 and MCM9 form a functional helicase complex (MCM8/9) that plays an essential role in DNA homologous recombination repair for DNA double-strand break. However, the structural characterization of MCM8/9 for DNA binding/unwinding remains unclear. Here, we report structures of the MCM8/9 complex using cryo-electron microscopy single particle analysis. The structures reveal that MCM8/9 is arranged into a heterohexamer through a threefold symmetry axis, creating a central channel that accommodates DNA. Multiple characteristic hairpins from the N-terminal oligosaccharide/oligonucleotide (OB) domains of MCM8/9 protrude into the central channel and serve to unwind the duplex DNA. When activated by HROB, the structure of MCM8/9's N-tier ring converts its symmetry from to with a conformational change that expands the MCM8/9's trimer interface. Moreover, our structural dynamic analyses revealed that the flexible C-tier ring exhibited rotary motions relative to the N-tier ring, which is required for the unwinding ability of MCM8/9. In summary, our structural and biochemistry study provides a basis for understanding the DNA unwinding mechanism of MCM8/9 helicase in homologous recombination.

PubMed: 37535404
DOI: 10.7554/eLife.87468

実験手法

ELECTRON MICROSCOPY (3.95 Å)