Płochocka D, Wełnicki M, Zielenkiewicz P, Ostoja-Zagórski W
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Proc Natl Acad Sci U S A. 1996 Oct 29;93(22):12150-4. doi: 10.1073/pnas.93.22.12150.
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.
已确定位于马铃薯Y病毒(普通株系)基因组中部的基因组连接病毒蛋白(VPg)顺反子的完整序列。VPg基因编码一种由188个氨基酸组成的蛋白质,与其他已知的马铃薯Y病毒属病毒VPg多肽具有显著同源性。基于疏水-亲水残基分布与已知晶体结构的苹果酸脱氢酶序列的相似性,提出了VPg的三维模型结构。病毒RNA的5′末端可通过Tyr-64暴露的羟基与该蛋白相互作用,这与实验数据一致。该复合物在立体化学上有利于形成小核糖核酸病毒样病毒代表典型的磷酸二酯键[5′-(O4-酪氨酰磷酸)腺苷酸]。基于蛋白质-RNA复合物的模型结构,讨论了病毒RNA与VPg结合的化学机制。