8wh6

MPOX E5 hexamer ADP and ssDNA bound and clear primase domain conformation

spinqualitylabelsall models 8wh6, resolution 3.27Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8wh6 is a 7 chain structure with sequence from Monkeypox virus and Spodoptera frugiperda. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.27Å Ligands: ADP, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5IXS3_MONPV Publication Abstract from PubMed 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(249), Lys(286), Lys(315), and Lys(317). 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. Essential and multifunctional mpox virus E5 helicase-primase in double and single hexamer.,Xu Y, Wu Y, Zhang Y, Gao K, Wu X, Yang Y, Li D, Yang B, Zhang Z, Dong C Sci Adv. 2024 Aug 23;10(34):eadl1150. doi: 10.1126/sciadv.adl1150. Epub 2024 Aug , 21. PMID:39167653 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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