View source for 6cgr


==CryoEM structure of herpes simplex virus 1 capsid with associated tegument protein complexes.==
<SX load='6cgr' size='340' side='right' viewer='molstar' caption='[[6cgr]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6cgr]] is a 51 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1 Human alphaherpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CGR 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]] 4.2&#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=6cgr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgr OCA], [https://pdbe.org/6cgr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cgr RCSB], [https://www.ebi.ac.uk/pdbsum/6cgr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgr ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/G8HBD2_HHV11 G8HBD2_HHV11] 
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== Publication Abstract from PubMed ==
Herpes simplex viruses (HSVs) rely on capsid-associated tegument complex (CATC) for long-range axonal transport of their genome-containing capsids between sites of infection and neuronal cell bodies. Here we report cryo-electron microscopy structures of the HSV-1 capsid with CATC up to 3.5-angstrom resolution and atomic models of multiple conformers of capsid proteins VP5, VP19c, VP23, and VP26 and tegument proteins pUL17, pUL25, and pUL36. Crowning every capsid vertex are five copies of heteropentameric CATC, each containing a pUL17 monomer supporting the coiled-coil helix bundle of a pUL25 dimer and a pUL36 dimer, thus positioning their flexible domains for potential involvement in nuclear capsid egress and axonal capsid transport. Notwithstanding newly discovered fold conservation between triplex proteins and bacteriophage lambda protein gpD and the previously recognized bacteriophage HK97 gp5-like fold in VP5, HSV-1 capsid proteins exhibit extraordinary diversity in forms of domain insertion and conformational polymorphism, not only for interactions with tegument proteins but also for encapsulation of large genomes.

Structure of the herpes simplex virus 1 capsid with associated tegument protein complexes.,Dai X, Zhou ZH Science. 2018 Apr 6;360(6384). pii: 360/6384/eaao7298. doi:, 10.1126/science.aao7298. Epub 2018 Apr 5. PMID:29622628<ref>PMID:29622628</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6cgr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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[[Category: Human alphaherpesvirus 1]]
[[Category: Large Structures]]
[[Category: Dai XH]]
[[Category: Zhou ZH]]