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. 1996 Oct 29;93(22):12150–12154. doi: 10.1073/pnas.93.22.12150

Three-dimensional model of the potyviral genome-linked protein.

D Płochocka 1, M Wełnicki 1, P Zielenkiewicz 1, W Ostoja-Zagórski 1
PMCID: PMC37958  PMID: 8901548

Abstract

The full sequence of the genome-linked viral protein (VPg) cistron located in the central part of potato virus Y (common strain) genome has been identified. The VPg gene codes for a protein of 188 amino acids, with significant homology to other known potyviral VPg polypeptides. A three-dimensional model structure of VPg is proposed on the basis of similarity of hydrophobic-hydrophilic residue distribution to the sequence of malate dehydrogenase of known crystal structure. The 5' end of the viral RNA can be fitted to interact with the protein through the exposed hydroxyl group of Tyr-64, in agreement with experimental data. The complex favors stereochemically the formation of a phosphodiester bond [5'-(O4-tyrosylphospho)adenylate] typical for representatives of picornavirus-like viruses. The chemical mechanisms of viral RNA binding to VPg are discussed on the basis of the model structure of protein-RNA complex.

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Selected References

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