8WH2

MPOX E5 hexamer 2ATP, 2ADP, and ssDNA binding comformation

8WH2 の概要

• エントリーDOI: 10.2210/pdb8wh2/pdb
• EMDBエントリー: 37526
• 分子名称: Uncoating factor OPG117, DNA (5'-D(P*CP*CP*CP*CP*C)-3'), ADENOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: monkey pox, helicase, dna replication, complex, viral protein, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Monkeypox virus; 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 546152.09

構造登録者

Zhang, Z.,Dong, C. (登録日: 2023-09-22, 公開日: 2024-11-27, 最終更新日: 2025-07-02)

主引用文献

Xu, Y.,Wu, Y.,Zhang, Y.,Gao, K.,Wu, X.,Yang, Y.,Li, D.,Yang, B.,Zhang, Z.,Dong, C.
Essential and multifunctional mpox virus E5 helicase-primase in double and single hexamer.
Sci Adv, 10:eadl1150-eadl1150, 2024

PubMed Abstract: An outbreak of mpox virus in May 2022 has spread over 110 nonpandemic regions in the world, posing a great threat to global health. Mpox virus E5, a helicase-primase, plays an essential role in DNA replication, but the molecular mechanisms are elusive. Here, we report seven structures of mpox virus E5 in a double hexamer (DH) and six in single hexamer in different conformations, indicating a rotation mechanism for helicase and a coupling action for primase. The DH is formed through the interface of zinc-binding domains, and the central channel density indicates potential double-stranded DNA (dsDNA), which helps to identify dsDNA binding residues Arg, Lys, Lys, and Lys. Our work is important not only for understanding poxviral DNA replication but also for the development of novel therapeutics for serious poxviral infections including smallpox virus and mpox virus.

PubMed: 39167653
DOI: 10.1126/sciadv.adl1150

実験手法

ELECTRON MICROSCOPY (2.9 Å)