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TitleStructure of monkeypox virus DNA polymerase holoenzyme.
Journal, issue, pagesScience, Vol. 379, Issue 6627, Page 100-105, Year 2023
Publish dateJan 6, 2023
AuthorsQi Peng / Yufeng Xie / Lu Kuai / Han Wang / Jianxun Qi / George F Gao / Yi Shi /
PubMed AbstractThe World Health Organization declared mpox (or monkeypox) a public health emergency of international concern in July 2022, and prophylactic and therapeutic measures are in urgent need. The monkeypox ...The World Health Organization declared mpox (or monkeypox) a public health emergency of international concern in July 2022, and prophylactic and therapeutic measures are in urgent need. The monkeypox virus (MPXV) has its own DNA polymerase F8, together with the processive cofactors A22 and E4, constituting the polymerase holoenzyme for genome replication. Here, we determined the holoenzyme structure in complex with DNA using cryo-electron microscopy at the global resolution of ~2.8 angstroms. The holoenzyme possesses an architecture that suggests a "forward sliding clamp" processivity mechanism for viral DNA replication. MPXV polymerase has a DNA binding mode similar to that of other B-family DNA polymerases from different species. These findings reveal the mechanism of the MPXV genome replication and may guide the development of anti-poxvirus drugs.
External linksScience / PubMed:36520947
MethodsEM (single particle)
Resolution2.8 Å
Structure data

34731

8hg1

EMDB-34731, PDB-8hg1:
The structure of MPXV polymerase holoenzyme in replicating state
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-TTP:
THYMIDINE-5'-TRIPHOSPHATE

Source
  • monkeypox virus
KeywordsREPLICATION/DNA / MPXV / Polymerase / Replication / REPLICATION-DNA complex

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