8HWC

Cryo-EM Structure of D5 Apo

8HWC の概要

• エントリーDOI: 10.2210/pdb8hwc/pdb
• EMDBエントリー: 35053
• 分子名称: Primase D5 (1 entity in total)
• 機能のキーワード: mpvx, viral protein
• 由来する生物種: Monkeypox virus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 542858.06

構造登録者

Li, Y.N.,Zhu, J.,Guo, Y.Y.,Yan, R.H. (登録日: 2022-12-29, 公開日: 2024-01-10, 最終更新日: 2024-01-31)

主引用文献

Li, Y.,Zhu, J.,Guo, Y.,Yan, R.
Structural insight into the assembly and working mechanism of helicase-primase D5 from Mpox virus.
Nat.Struct.Mol.Biol., 31:68-81, 2024

PubMed Abstract: The Mpox pandemic, caused by the Mpox virus (or monkeypox virus, MPXV), has gained global attention. The D5 protein, a putative helicase-primase found in MPXV, plays a vital role in viral replication and genome uncoating. Here we determined multiple cryo-EM structures of full-length hexameric D5 in diverse states. These states were captured during ATP hydrolysis while moving along the single-stranded DNA (ssDNA) track. Through comprehensive structural analysis combined with the helicase activity system, we revealed that when the primase domain is truncated or the interaction between the primase and helicase domains is disrupted, the double-stranded DNA (dsDNA) unwinds into ssDNA, suggesting a critical regulatory role of the primase domain. Two transition states bound with ssDNA substrate during unwinding reveals that two ATP molecules were consumed to drive DNA moving forward two nucleotides. Collectively, our findings shed light on the molecular mechanism that links ATP hydrolysis to the DNA unwinding in poxviruses.

PubMed: 38177671
DOI: 10.1038/s41594-023-01142-0

実験手法

ELECTRON MICROSCOPY (3.3 Å)