9zm2: Difference between revisions
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==Human cytomegalovirus UL52 4-mer== | |||
<StructureSection load='9zm2' size='340' side='right'caption='[[9zm2]], [[Resolution|resolution]] 3.29Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9zm2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_betaherpesvirus_5 Human betaherpesvirus 5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9ZM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9ZM2 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]] 3.29Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=9zm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9zm2 OCA], [https://pdbe.org/9zm2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9zm2 RCSB], [https://www.ebi.ac.uk/pdbsum/9zm2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9zm2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/UL52_HCMVA UL52_HCMVA] Plays a role in efficient localization of neo-synthesized capsids to nuclear replication compartments, thereby controlling cleavage and packaging of virus genomic DNA.<ref>PMID:18077717</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
To create a new wave of infectious virions, all herpesviruses require an accessory factor of unknown function to package their viral genomes into nascent capsids. Here, we present cryo-EM structures of the packaging accessory factor from the alpha-herpesvirus herpes simplex virus type 1 (HSV-1, UL32) and the beta-herpesvirus human cytomegalovirus (HCMV, UL52). Unlike homologs from the gamma-herpesviruses, neither UL32 nor UL52 form stable homopentameric rings. UL52 forms incomplete pentameric rings lacking one or two protomers. UL32 does not form stable higher-order species, but stabilization through chemical crosslinking revealed a novel quaternary structure where three pentameric rings assemble into a "tripentamer." Our results reveal that herpesvirus packaging accessory factors adopt distinct oligomeric states but are constrained to pentameric symmetry. Assembly of protomers into a ring creates a positively charged central channel that we show is critical for infectious virus production in HSV-1. Taken together, our study points to a structurally conserved, essential function of packaging accessory factors across the Herpesviridae. | |||
Conserved assembly architecture of the essential herpesvirus packaging accessory factor.,Bailey EJ, Devarkar SC, Szczepaniak R, Meissner LM, Chen X, Wu C, Weller SK, Xiong Y, Didychuk AL bioRxiv [Preprint]. 2026 Jan 22:2026.01.22.701024. doi: , 10.64898/2026.01.22.701024. PMID:41648366<ref>PMID:41648366</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 9zm2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human betaherpesvirus 5]] | |||
[[Category: Large Structures]] | |||
[[Category: Bailey EJ]] | |||
[[Category: Devarkar SC]] | |||
[[Category: Didychuk AL]] | |||
[[Category: Xiong Y]] | |||
