View source for 7og6


==Structure of Alternanthera Mosaic VLP by cryoEM==
<StructureSection load='7og6' size='340' side='right'caption='[[7og6]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7og6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Alternanthera_mosaic_virus Alternanthera mosaic virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OG6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OG6 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]] 3.3&#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=7og6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7og6 OCA], [https://pdbe.org/7og6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7og6 RCSB], [https://www.ebi.ac.uk/pdbsum/7og6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7og6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q52Z61_9VIRU Q52Z61_9VIRU] Required for genome encapsidation. Forms ribonucleoprotein complexes along with TGB1 helicase and viral RNA.[ARBA:ARBA00004032]
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== Publication Abstract from PubMed ==
The production of plant helical virus-like particles (VLPs) via plant-based expression has been problematic with previous studies suggesting that an RNA scaffold may be necessary for their efficient production. To examine this, we compared the accumulation of VLPs from two potexviruses, papaya mosaic virus and alternanthera mosaic virus (AltMV), when the coat proteins were expressed from a replicating potato virus X- based vector (pEff) and a non-replicating vector (pEAQ-HT). Significantly greater quantities of VLPs could be purified when pEff was used. The pEff system was also very efficient at producing VLPs of helical viruses from different virus families. Examination of the RNA content of AltMV and tobacco mosaic virus VLPs produced from pEff revealed the presence of vector-derived RNA sequences, suggesting that the replicating RNA acts as a scaffold for VLP assembly. Cryo-EM analysis of the AltMV VLPs showed they had a structure very similar to that of authentic potexvirus particles. Thus, we conclude that vectors generating replicating forms of RNA, such as pEff, are very efficient for producing helical VLPs.

A Replicating Viral Vector Greatly Enhances Accumulation of Helical Virus-Like Particles in Plants.,Thuenemann EC, Byrne MJ, Peyret H, Saunders K, Castells-Graells R, Ferriol I, Santoni M, Steele JFC, Ranson NA, Avesani L, Lopez-Moya JJ, Lomonossoff GP Viruses. 2021 May 11;13(5):885. doi: 10.3390/v13050885. PMID:34064959<ref>PMID:34064959</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Tobacco Mosaic Virus|Tobacco Mosaic Virus]]
*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Alternanthera mosaic virus]]
[[Category: Large Structures]]
[[Category: Byrne MJ]]
[[Category: Lomonossoff GP]]
[[Category: Ranson NA]]
[[Category: Thuenemann EC]]