7YZV
Ryegrass mottle virus serine protease domain S159A mutant
Summary for 7YZV
| Entry DOI | 10.2210/pdb7yzv/pdb |
| Related | 6FEZ 6FF0 |
| Descriptor | RNA-directed RNA polymerase (2 entities in total) |
| Functional Keywords | serine protease, viral protease, viral polypeptide, viral genome-linked protein, viral protein |
| Biological source | Ryegrass mottle virus |
| Total number of polymer chains | 1 |
| Total formula weight | 20867.98 |
| Authors | Kalnins, G. (deposition date: 2022-02-21, release date: 2022-03-02, Last modification date: 2024-11-06) |
| 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 Cited by 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: 36982419DOI: 10.3390/ijms24065347 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
Download full validation report
