Structural highlights
Function[A0A0B6VPI0_EBVG] Forms a portal in the viral capsid through which viral DNA is translocated during DNA packaging. Assembles as a dodecamer at a single fivefold axe of the T=16 icosahedric capsid. Binds to the molecular motor that translocates the viral DNA, termed terminase.[HAMAP-Rule:MF_04012] Publication Abstract from PubMedHerpesviridae is a vast family of enveloped DNA viruses that includes eight distinct human pathogens, responsible for diseases that range from almost asymptomatic to severe and life-threatening. Epstein-Barr virus infects B-cells and epithelial cells, causing infectious mononucleosis, as well as a number of cancers. Epstein-Barr infection cannot be cured since neither vaccine nor antiviral drug treatments are available. All herpesviruses contain a linear double-stranded DNA genome, enclosed within an icosahedral capsid. Viral portal protein plays a key role in the procapsid assembly and DNA packaging. The portal is the entrance and exit pore for the viral genome, making it an attractive pharmacological target for the development of new antivirals. Here we present the atomic structure of the portal protein of Epstein-Barr virus, solved by cryo-electron microscopy at 3.5 A resolution. The detailed architecture of this protein suggests that it plays a functional role in DNA retention during packaging. Atomic structure of the Epstein-Barr virus portal.,Machon C, Fabrega-Ferrer M, Zhou D, Cuervo A, Carrascosa JL, Stuart DI, Coll M Nat Commun. 2019 Aug 29;10(1):3891. doi: 10.1038/s41467-019-11706-8. PMID:31467275[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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