Essential and multifunctional mpox virus E5 helicase-primase in double and single hexamer.

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 Arg²⁴⁹, Lys²⁸⁶, Lys³¹⁵, and Lys³¹⁷. Our work is important not only for understanding poxviral DNA repl

SUBMITTER: Xu Y 

PROVIDER: S-EPMC11338233 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature