We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
7bqt
From Proteopedia
(Difference between revisions)
| (3 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Epstein-Barr virus, C12 portal dodecamer== | |
| + | <StructureSection load='7bqt' size='340' side='right'caption='[[7bqt]], [[Resolution|resolution]] 4.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BQT 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]] 4.8Å</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=7bqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bqt OCA], [https://pdbe.org/7bqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bqt RCSB], [https://www.ebi.ac.uk/pdbsum/7bqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bqt ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <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> |
| - | [[Category: | + | <div class="pdbe-citations 7bqt" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | |
| + | ==See Also== | ||
| + | *[[Portal protein 3D structures|Portal protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Li Z]] | ||
| + | [[Category: Yu X]] | ||
Current revision
Epstein-Barr virus, C12 portal dodecamer
| |||||||||||
