View source for 9oac


==C5 reconstruction of the thermophilic bacteriophage P74-26 Portal Vertex==
<StructureSection load='9oac' size='340' side='right'caption='[[9oac]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9oac]] is a 55 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_virus_P74-26 Thermus virus P74-26]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9OAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9OAC 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]] 2.6&#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=9oac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9oac OCA], [https://pdbe.org/9oac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9oac RCSB], [https://www.ebi.ac.uk/pdbsum/9oac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9oac ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A7XXR6_BP742 A7XXR6_BP742] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Viruses assemble from component parts inside their host cells, but the mechanisms coordinating this complex process are not completely understood. In tailed bacteriophages, the genome is packaged into its capsid shell through the portal complex. The portal complex then closes to retain DNA and connects to the tail, which is required for host recognition and infection. The trigger to stop pumping DNA and assemble the mature virus has been a longstanding conundrum in the field. We determined the structure of the portal, the proteins that connect it to the tail, and portal vertex in the hyperthermophilic phage Oshimavirus using cryo-Electron Microscopy (cryo-EM). We find highly intertwined loop structures, like in a wicker basket, potentially stabilizing the portal vertex against high temperatures. Moreover, we observe that the portal protrudes from the capsid in mature virions. We propose that portal is repositioned by packaged DNA, forming a pressure-sensitive switch that terminates genome packaging and triggers tail attachment in headful phages.

The Structure of a Thermostable Phage's Portal Vertex and Neck Complex Illuminates the Headful Maturation Mechanism.,Sedivy EL, Agnello E, Hobaugh JE, Ahsan R, Song K, Xu C, Kelch BA J Mol Biol. 2026 Jan 14;438(6):169641. doi: 10.1016/j.jmb.2026.169641. PMID:41544933<ref>PMID:41544933</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9oac" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus virus P74-26]]
[[Category: Agnello E]]
[[Category: Kelch BA]]
[[Category: Sedivy EL]]
[[Category: Song K]]
[[Category: Xu C]]