ArticleScience advances2024
Essential and multifunctional mpox virus E5 helicase-primase in double and single hexamer.
Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Exploration of the protein and pharmacological landscape of monkeypox virus treatment: from entry point to end point.Molecular diversity · 2026Review
- In situ structure of the poxvirus portal complex.Nature · 2026Article
- Monkeypox (Mpox), a Resurging Global Public Health Concern: An Updated Outlook Through 2025.Current issues in molecular biology · 2026Review
- Structural and mechanistic insights into the herpes simplex virus type 1 helicase-primase primosome.Cell discovery · 2025Article
- Evaluating the Antiviral Potential of Polyherbal Formulation (Life (Basel, Switzerland) · 2025Article
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
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
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