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Structure and operating principles of a monkeypox virus replisome

Research Structural Biology

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TL;DR - This Nature study describes the structure and activation mechanism of the monkeypox virus replisome. It reveals how assembly-driven conformational changes in the E5 helicase–primase enable interactions that activate viral DNA replication machinery.

  • The helicase–primase E5 forms a hexamer within the monkeypox virus replisome.
  • Replisome assembly triggers large-scale conformational changes in E5.
  • Two E5 primase domains contact the F8 polymerase thumb domain and the A22 subunit.
  • These interactions activate the helicase–primase, clarifying a key operating principle of poxvirus replication.

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Structure and operating principles of a monkeypox virus replisome

Nature Zishuo Yu, Pradeep Sathyanarayana, Joel M. J. Tan, Side Hu, Xiaoyi Fan, Angela Gao, Philip J. Kranzusch, Joseph J. Loparo, Jonathan Abraham 2026-09-02 doi:10.1038/s41586-026-10937-2
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Providers: Hugging Face · N/A OpenAlex · Citations 0 Publisher · N/A Semantic Scholar · N/A X · N/A Fetched 2026-09-25 14:23:38.585972 UTC

TL;DR - This Nature study describes the structure and activation mechanism of the monkeypox virus replisome. It reveals how assembly-driven conformational changes in the E5 helicase–primase enable interactions that activate viral DNA replication machinery.

  • The helicase–primase E5 forms a hexamer within the monkeypox virus replisome.
  • Replisome assembly triggers large-scale conformational changes in E5.
  • Two E5 primase domains contact the F8 polymerase thumb domain and the A22 subunit.
  • These interactions activate the helicase–primase, clarifying a key operating principle of poxvirus replication.
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