7br7

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== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/MCP_EBVB9 MCP_EBVB9] Self-assembles to form an icosahedral capsid with a T=16 symmetry, about 200 nm in diameter, and consisting of 150 hexons and 12 pentons (total of 162 capsomers). Hexons form the edges and faces of the capsid and are each composed of six MCP molecules. In contrast, one penton is found at each of the 12 vertices. Eleven of the pentons are MCP pentamers, while the last vertex is occupied by the portal complex. The capsid is surrounded by a layer of proteinaceous material designated the tegument which, in turn, is enclosed in an envelope of host cell-derived lipids containing virus-encoded glycoproteins.[HAMAP-Rule:MF_04016]<ref>PMID:19158247</ref>
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[https://www.uniprot.org/uniprot/CVC2_EBVB9 CVC2_EBVB9] Capsid vertex-specific component that plays a role during viral DNA encapsidation, assuring correct genome cleavage and presumably stabilizing capsids that contain full-length viral genomes. Participates in the interaction between the capsid and the tegument through interaction with the large tegument protein/LTP.[HAMAP-Rule:MF_04025]
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== Publication Abstract from PubMed ==
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Epstein-Barr virus (EBV) is the primary cause of infectious mononucleosis and has been shown to be closely associated with various malignancies. Here, we present a complete atomic model of EBV, including the icosahedral capsid, the dodecameric portal and the capsid-associated tegument complex (CATC). Our in situ portal from the tegumented capsid adopts a closed conformation with its channel valve holding the terminal viral DNA and with its crown region firmly engaged by three layers of ring-like dsDNA, which, together with the penton flexibility, effectively alleviates the capsid inner pressure placed on the portal cap. In contrast, the CATCs, through binding to the flexible penton vertices in a stoichiometric manner, accurately increase the inner capsid pressure to facilitate the pressure-driven genome delivery. Together, our results provide important insights into the mechanism by which the EBV capsid, portal, packaged genome and the CATCs coordinately achieve a pressure balance to simultaneously benefit both viral genome retention and ejection.
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CryoEM structure of the tegumented capsid of Epstein-Barr virus.,Li Z, Zhang X, Dong L, Pang J, Xu M, Zhong Q, Zeng MS, Yu X Cell Res. 2020 Jul 3. pii: 10.1038/s41422-020-0363-0. doi:, 10.1038/s41422-020-0363-0. PMID:32620850<ref>PMID:32620850</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
== References ==
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Current revision

Epstein-Barr virus, C1 portal-proximal penton vertex, CATC binding

PDB ID 7br7

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