7br7
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Epstein-Barr virus, C1 portal-proximal penton vertex, CATC binding== |
| - | <StructureSection load='7br7' size='340' side='right'caption='[[7br7]]' scene=''> | + | <StructureSection load='7br7' size='340' side='right'caption='[[7br7]], [[Resolution|resolution]] 4.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[7br7]] is a 21 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=7BR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BR7 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.3Å</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=7br7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7br7 OCA], [https://pdbe.org/7br7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7br7 RCSB], [https://www.ebi.ac.uk/pdbsum/7br7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7br7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [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> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human herpesvirus 4 strain B95-8]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Z | + | [[Category: Li Z]] |
| + | [[Category: Yu X]] | ||
Revision as of 10:49, 27 March 2024
Epstein-Barr virus, C1 portal-proximal penton vertex, CATC binding
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