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== Function ==

[https://www.uniprot.org/uniprot/A0MCW0_9VIRU A0MCW0_9VIRU]

== Publication Abstract from PubMed ==

Sobemoviruses encode serine-like 3C proteases (Pro) that participate in the processing and maturation of other virus-encoded proteins. Its cis and trans activity is mediated by the naturally unfolded virus-genome-linked protein (VPg). Nuclear magnetic resonance studies show a Pro-VPg complex interaction and VPg tertiary structure; however, information regarding structural changes of the Pro-VPg complex during interaction is lacking. Here, we solved a full Pro-VPg 3D structure of ryegrass mottle virus (RGMoV) that demonstrates the structural changes in three different conformations due to VPg interaction with Pro. We identified a unique site of VPg interaction with Pro that was not observed in other sobemoviruses, and observed different conformations of the Pro beta2 barrel. This is the first report of a full plant Pro crystal structure with its VPg cofactor. We also confirmed the existence of an unusual previously unmapped cleavage site for sobemovirus Pro in the transmembrane domain: E/A. We demonstrated that RGMoV Pro in cis activity is not regulated by VPg and that in trans, VPg can also mediate Pro in free form. Additionally, we observed Ca(2+) and Zn(2+) inhibitory effects on the Pro cleavage activity.

VPg Impact on Ryegrass Mottle Virus Serine-like 3C Protease Proteolysis and Structure.,Kalnins G, Ludviga R, Kalnciema I, Resevica G, Zeltina V, Bogans J, Tars K, Zeltins A, Balke I Int J Mol Sci. 2023 Mar 10;24(6):5347. doi: 10.3390/ijms24065347. PMID:36982419<ref>PMID:36982419</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

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 == Function ==
 [https://www.uniprot.org/uniprot/A0MCW0_9VIRU A0MCW0_9VIRU]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Sobemoviruses encode serine-like 3C proteases (Pro) that participate in the processing and maturation of other virus-encoded proteins. Its cis and trans activity is mediated by the naturally unfolded virus-genome-linked protein (VPg). Nuclear magnetic resonance studies show a Pro-VPg complex interaction and VPg tertiary structure; however, information regarding structural changes of the Pro-VPg complex during interaction is lacking. Here, we solved a full Pro-VPg 3D structure of ryegrass mottle virus (RGMoV) that demonstrates the structural changes in three different conformations due to VPg interaction with Pro. We identified a unique site of VPg interaction with Pro that was not observed in other sobemoviruses, and observed different conformations of the Pro beta2 barrel. This is the first report of a full plant Pro crystal structure with its VPg cofactor. We also confirmed the existence of an unusual previously unmapped cleavage site for sobemovirus Pro in the transmembrane domain: E/A. We demonstrated that RGMoV Pro in cis activity is not regulated by VPg and that in trans, VPg can also mediate Pro in free form. Additionally, we observed Ca(2+) and Zn(2+) inhibitory effects on the Pro cleavage activity.
+VPg Impact on Ryegrass Mottle Virus Serine-like 3C Protease Proteolysis and Structure.,Kalnins G, Ludviga R, Kalnciema I, Resevica G, Zeltina V, Bogans J, Tars K, Zeltins A, Balke I Int J Mol Sci. 2023 Mar 10;24(6):5347. doi: 10.3390/ijms24065347. PMID:36982419<ref>PMID:36982419</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6ff0" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>