View source for 9r81


==ssRNA-containing helical virus-like particle composed of PVA coat protein with D138C mutation==
<StructureSection load='9r81' size='340' side='right'caption='[[9r81]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9r81]] is a 72 chain structure with sequence from [https://en.wikipedia.org/wiki/Potato_virus_A Potato virus A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9R81 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9R81 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]] 2.33&#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=9r81 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9r81 OCA], [https://pdbe.org/9r81 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9r81 RCSB], [https://www.ebi.ac.uk/pdbsum/9r81 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9r81 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O11986_PVMA O11986_PVMA] Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.[ARBA:ARBA00029405]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Potyviruses are the largest group of plant positive-sense single-stranded RNA viruses and represent a major economic burden worldwide. Their coat protein (CP) forms a filamentous, flexible capsid around the genomic RNA. However, information is still lacking on the mechanisms of virion assembly, disassembly and stability, which is central to understanding virus biology and control. Here, we investigate the role of CP in these processes using structural, biochemical and biophysical studies of five potyviral CPs from three phylogenetic clades combined with bioinformatics and in planta experiments. Our results suggest that, while potyviruses have a conserved virion structure, the amino acids forming the CP-CP and CP-RNA interactions leading to this structure are species-specific. We show that the species-specific CP sequence also determines the architecture of RNA-free virus-like particles (VLPs) and the degree of their structural polymorphism. We identify the residues that determine this specificity at distinct S1-S4 interaction sites. In contrast, a highly conserved charged amino acid triad at the CP-CP interface is essential for the stability of virions and RNA-free VLPs. These results contribute to understanding the molecular mechanism of potyviral virion assembly and highlight the significance of the amino acid sequence of selected CPs in potential biotechnological or biomedical applications.

Species-specific structural adaptation of the potyviral coat protein in virions and virus-like particles.,Koritnik N, Kezar A, Kavcic L, Znidaric MT, Leonardi A, De S, Pollari M, Makinen K, Podobnik M Commun Biol. 2026 Jan 13. doi: 10.1038/s42003-025-09502-w. PMID:41530503<ref>PMID:41530503</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9r81" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Potato virus A]]
[[Category: Kezar A]]
[[Category: Koritnik N]]
[[Category: Podobnik M]]