VPg Impact on Ryegrass Mottle Virus Serine-like 3C Protease Proteolysis and Structure.

ABSTRACT: 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 β2 barrel. This

SUBMITTER: Kalnins G 

PROVIDER: S-EPMC10048871 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature