View source for 6ppb


==Kaposi's sarcoma-associated herpesvirus (KSHV), C5 portal vertex structure==
<SX load='6ppb' size='340' side='right' viewer='molstar' caption='[[6ppb]], [[Resolution|resolution]] 4.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ppb]] is a 19 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_herpesvirus_8_strain_GK18 Human herpesvirus 8 strain GK18]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PPB 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]] 4.3&#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=6ppb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ppb OCA], [https://pdbe.org/6ppb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ppb RCSB], [https://www.ebi.ac.uk/pdbsum/6ppb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ppb ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/CVC1_HHV8P CVC1_HHV8P] 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 ==
Assembly of Kaposi's sarcoma-associated herpesvirus (KSHV) begins at a bacteriophage-like portal complex that nucleates formation of an icosahedral capsid with capsid-associated tegument complexes (CATCs) and facilitates translocation of an approximately 150-kb dsDNA genome, followed by acquisition of a pleomorphic tegument and envelope. Because of deviation from icosahedral symmetry, KSHV portal and tegument structures have largely been obscured in previous studies. Using symmetry-relaxed cryo-EM, we determined the in situ structure of the KSHV portal and its interactions with surrounding capsid proteins, CATCs, and the terminal end of KSHV's dsDNA genome. Our atomic models of the portal and capsid/CATC, together with visualization of CATCs' variable occupancy and alternate orientation of CATC-interacting vertex triplexes, suggest a mechanism whereby the portal orchestrates procapsid formation and asymmetric long-range determination of CATC attachment during DNA packaging prior to pleomorphic tegumentation/envelopment. Structure-based mutageneses confirm that a triplex deep binding groove for CATCs is a hotspot that holds promise for antiviral development.

DNA-Packing Portal and Capsid-Associated Tegument Complexes in the Tumor Herpesvirus KSHV.,Gong D, Dai X, Jih J, Liu YT, Bi GQ, Sun R, Zhou ZH Cell. 2019 Sep 5;178(6):1329-1343.e12. doi: 10.1016/j.cell.2019.07.035. Epub 2019, Aug 22. PMID:31447177<ref>PMID:31447177</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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[[Category: Human herpesvirus 8 strain GK18]]
[[Category: Large Structures]]
[[Category: Bi GQ]]
[[Category: Dai X]]
[[Category: Gong D]]
[[Category: Jih J]]
[[Category: Liu YT]]
[[Category: Sun R]]
[[Category: Zhou ZH]]