View source for 8heu


==C12 portal in HCMV A-capsid==
<StructureSection load='8heu' size='340' side='right'caption='[[8heu]], [[Resolution|resolution]] 4.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8heu]] is a 12 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=8HEU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HEU 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]] 4.6&#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=8heu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8heu OCA], [https://pdbe.org/8heu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8heu RCSB], [https://www.ebi.ac.uk/pdbsum/8heu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8heu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PORTL_HCMVA PORTL_HCMVA] Forms a portal in the viral capsid through which viral DNA is translocated during DNA packaging. Assembles as a dodecamer at a single fivefold axe of the T=16 icosahedric capsid. Binds to the molecular motor that translocates the viral DNA, termed terminase.[HAMAP-Rule:MF_04012]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The portal-scaffold complex is believed to nucleate the assembly of herpesvirus procapsids. During capsid maturation, two events occur: scaffold expulsion and DNA incorporation. The portal-scaffold interaction and the conformational changes that occur to the portal during the different stages of capsid formation have yet to be elucidated structurally. Here we present high-resolution structures of the A- and B-capsids and in-situ portals of human cytomegalovirus. We show that scaffolds bind to the hydrophobic cavities formed by the dimerization and Johnson-fold domains of the major capsid proteins. We further show that 12 loop-helix-loop fragments-presumably from the scaffold domain-insert into the hydrophobic pocket of the portal crown domain. The portal also undergoes significant changes both positionally and conformationally as it accompanies DNA packaging. These findings unravel the mechanism by which the portal interacts with the scaffold to nucleate capsid assembly and further our understanding of scaffold expulsion and DNA incorporation.

Cryo-electron microscopy structures of capsids and in situ portals of DNA-devoid capsids of human cytomegalovirus.,Li Z, Pang J, Gao R, Wang Q, Zhang M, Yu X Nat Commun. 2023 Apr 11;14(1):2025. doi: 10.1038/s41467-023-37779-0. PMID:37041152<ref>PMID:37041152</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 8heu" style="background-color:#fffaf0;"></div>

==See Also==
*[[Portal protein 3D structures|Portal protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human herpesvirus 5 strain AD169]]
[[Category: Large Structures]]
[[Category: Li Z]]
[[Category: Yu X]]