9R7S
Potato virus A (PVA) after incubation in solution at 4C for 6 months
This is a non-PDB format compatible entry.
Summary for 9R7S
| Entry DOI | 10.2210/pdb9r7s/pdb |
| EMDB information | 53790 53791 |
| Descriptor | Capsid protein, RNA (5'-R(P*UP*UP*UP*UP*U)-3') (2 entities in total) |
| Functional Keywords | potato virus a, potyvirus, coat protein, rna, helical, virus |
| Biological source | Potato virus A More |
| Total number of polymer chains | 72 |
| Total formula weight | 1148951.99 |
| Authors | Koritnik, N.,Kezar, A.,Podobnik, M. (deposition date: 2025-05-15, release date: 2026-01-21, Last modification date: 2026-02-25) |
| Primary citation | Koritnik, N.,Kezar, A.,Kavcic, L.,Znidaric, M.T.,Leonardi, A.,De, S.,Pollari, M.,Makinen, K.,Podobnik, M. Species-specific structural adaptation of the potyviral coat protein in virions and virus-like particles. Commun Biol, 9:226-226, 2026 Cited by PubMed Abstract: 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. PubMed: 41530503DOI: 10.1038/s42003-025-09502-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.54 Å) |
Structure validation
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