View source for 7br8


==Epstein-Barr virus, C5 penton vertex, CATC absent.==
<StructureSection load='7br8' size='340' side='right'caption='[[7br8]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7br8]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_herpesvirus_4_strain_B95-8 Human herpesvirus 4 strain B95-8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BR8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7br8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7br8 OCA], [https://pdbe.org/7br8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7br8 RCSB], [https://www.ebi.ac.uk/pdbsum/7br8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7br8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SCP_EBVB9 SCP_EBVB9] Participates in the assembly of the infectious particles by decorating the outer surface of the capsid shell and thus forming a layer between the capsid and the tegument. Complexes composed of the major capsid protein and small capsomere-interacting protein/SCP assemble together in the host cytoplasm and are translocated to the nucleus, where they accumulate and participate in capsid assembly.[HAMAP-Rule:MF_04022]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7br8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Human herpesvirus 4 strain B95-8]]
[[Category: Large Structures]]
[[Category: Li Z]]
[[Category: Yu X]]