6FEZ

Ryegrass mottle virus protease domain

Summary for 6FEZ

• Entry DOI: 10.2210/pdb6fez/pdb
• Descriptor: Serine protease domain (2 entities in total)
• Functional Keywords: serine protease, viral protease, viral protein
• Biological source: Ryegrass mottle virus
• Total number of polymer chains: 2
• Total formula weight: 41767.96

Authors

Kalnins, G. (deposition date: 2018-01-03, release date: 2019-04-17, Last modification date: 2024-11-13)

Primary citation

Kalnins, G.,Ludviga, R.,Kalnciema, I.,Resevica, G.,Zeltina, V.,Bogans, J.,Tars, K.,Zeltins, A.,Balke, I.
VPg Impact on Ryegrass Mottle Virus Serine-like 3C Protease Proteolysis and Structure.
Int J Mol Sci, 24:-, 2023

PubMed Abstract: Sobemoviruses encode serine-like 3C proteases (Pro) that participate in the processing and maturation of other virus-encoded proteins. Its and 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 β2 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 activity is not regulated by VPg and that , VPg can also mediate Pro in free form. Additionally, we observed Ca and Zn inhibitory effects on the Pro cleavage activity.

PubMed: 36982419
DOI: 10.3390/ijms24065347

Experimental method

X-RAY DIFFRACTION (2.3 Å)