8xj6
From Proteopedia
The Cryo-EM structure of MPXV E5 apo conformation
Structural highlights
FunctionPG117_MONPV Multifunctional protein required for genome uncoating and replication. Major viral uncoating protein that is required for the release of the viral genome from incoming viral cores containing the viral DNA genome. Possesses an ATPase activity that is required for hexamerization and uncoating.[UniProtKB:P04305] Publication Abstract from PubMedMpox virus (MPXV) can cause mpox in humans. Due to its quick and wide spread in the past two years, mpox has turned into a significant public health concern. Helicase E5 is a multi-domain protein; its primer synthesis and DNA unwinding activity are required for genome uncoating and DNA replication of MPXV. However, the in vitro DNA unwinding activity has never been demonstrated. Here, we report the structural and biochemical studies of MPXV E5, showing that the full-length protein adopts an auto-inhibited conformation. Truncation of the N-terminus can recover the in vitro unwinding activity of E5 towards the forked DNA. Further structural analysis reveals that MPXV E5 shares a conserved mechanism in DNA unwinding and primer synthesis with the homologous proteins. These findings not only advance our understanding on the function of MPXV E5, but also provide a solid basis for the development of anti-poxvirus drugs. Structural and functional insights into the helicase protein E5 of Mpox virus.,Zhang W, Liu Y, Yang M, Yang J, Shao Z, Gao Y, Jiang X, Cui R, Zhang Y, Zhao X, Shao Q, Cao C, Li H, Li L, Liu H, Gao H, Gan J Cell Discov. 2024 Jun 25;10(1):67. doi: 10.1038/s41421-024-00680-1. PMID:38914567[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Large Structures | Monkeypox virus | Gan J | Gao H | Liu Y | Zhang W
