View source for 8rt0


==BTV-15 VP5 pH 6.0==
<StructureSection load='8rt0' size='340' side='right'caption='[[8rt0]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8rt0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bluetongue_virus Bluetongue virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8RT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RT0 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19&#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=8rt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rt0 OCA], [https://pdbe.org/8rt0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rt0 RCSB], [https://www.ebi.ac.uk/pdbsum/8rt0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rt0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/R4J9Y2_9REOV R4J9Y2_9REOV] VP5 protein is one of the two proteins (with VP2) which constitute the virus particle outer capsid. Acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. Permeabilization activity is probably negatively regulated by VP2 and is triggered by endosomal degradation of VP2 and exposure to low pH.[ARBA:ARBA00024835]
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== Publication Abstract from PubMed ==
The unenveloped Bluetongue virus capsid comprises several structural layers, the inner two comprising a core, which assembles before addition of the outer proteins, VP2 and VP5. Two symmetric trimers of VP5 fit like pegs into two distinct pits on the core and undergo pH conformational changes in the context of the virus, associated with cell entry. Here we show that in isolation VP5 alone undergoes essentially the same changes with pH and confirm a helical transition, indicating that VP5 is a motor during cell entry. In the absence of VP5 the two pits on the core differ from each other, presumably due to the asymmetric underlying structure of VP3, the innermost capsid protein. On insertion of VP5 these pits become closely similar and remain similar at low pH whilst VP5 is present. This natural asymmetry presumably destabilises the attachment of VP5, facilitating ejection upon low pH, membrane penetration and cell entry.

The effect of pH on the structure of Bluetongue virus VP5.,Zhang H, El Omari K, Sutton G, Stuart DI J Gen Virol. 2024 Aug;105(8):002018. doi: 10.1099/jgv.0.002018. PMID:39163113<ref>PMID:39163113</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8rt0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bluetongue virus]]
[[Category: Large Structures]]
[[Category: Stuart DI]]
[[Category: Sutton GC]]