View source for 8teu


==Human cytomegalovirus portal vertex, non-infectious enveloped particle (NIEP) configuration 2 - inverted (NC2-inv)==
<StructureSection load='8teu' size='340' side='right'caption='[[8teu]], [[Resolution|resolution]] 4.01&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8teu]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_herpesvirus_5_strain_AD169 Human herpesvirus 5 strain AD169]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8TEU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8TEU 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]] 4.01&#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=8teu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8teu OCA], [https://pdbe.org/8teu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8teu RCSB], [https://www.ebi.ac.uk/pdbsum/8teu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8teu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CVC1_HCMVA CVC1_HCMVA] 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.[HAMAP-Rule:MF_04017]
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== Publication Abstract from PubMed ==
The compartmentalization of eukaryotic cells presents considerable challenges to the herpesvirus life cycle. The herpesvirus tegument, a bulky proteinaceous aggregate sandwiched between herpesviruses' capsid and envelope, is uniquely evolved to address these challenges, yet tegument structure and organization remain poorly characterized. We use deep-learning-enhanced cryogenic electron microscopy to investigate the tegument of human cytomegalovirus virions and noninfectious enveloped particles (NIEPs; a genome packaging-aborted state), revealing a portal-biased tegumentation scheme. We resolve atomic structures of portal vertex-associated tegument (PVAT) and identify multiple configurations of PVAT arising from layered reorganization of pUL77, pUL48 (large tegument protein), and pUL47 (inner tegument protein) assemblies. Analyses show that pUL77 seals the last-packaged viral genome end through electrostatic interactions, pUL77 and pUL48 harbor a head-linker-capsid-binding motif conducive to PVAT reconfiguration, and pUL47/48 dimers form 45-nm-long filaments extending from the portal vertex. These results provide a structural framework for understanding how herpesvirus tegument facilitates and evolves during processes spanning viral genome packaging to delivery.

The incredible bulk: Human cytomegalovirus tegument architectures uncovered by AI-empowered cryo-EM.,Jih J, Liu YT, Liu W, Zhou ZH Sci Adv. 2024 Feb 23;10(8):eadj1640. doi: 10.1126/sciadv.adj1640. Epub 2024 Feb , 23. PMID:38394211<ref>PMID:38394211</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8teu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human herpesvirus 5 strain AD169]]
[[Category: Large Structures]]
[[Category: Jih J]]
[[Category: Liu W]]
[[Category: Liu YT]]
[[Category: Zhou H]]