7bqx
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Epstein-Barr virus, C5 portal vertex== | |
| + | <StructureSection load='7bqx' size='340' side='right'caption='[[7bqx]], [[Resolution|resolution]] 4.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7bqx]] is a 19 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=7BQX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BQX 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]] 4.2Å</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=7bqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bqx OCA], [https://pdbe.org/7bqx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bqx RCSB], [https://www.ebi.ac.uk/pdbsum/7bqx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bqx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TRX1_EBVB9 TRX1_EBVB9] Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly. | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7bqx" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human herpesvirus 4 strain B95-8]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Li Z]] | ||
| + | [[Category: Yu X]] | ||
Current revision
Epstein-Barr virus, C5 portal vertex
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