Johnson G P, Goebel S J, Perkus M E, Davis S W, Winslow J P, Paoletti E
Virogenetics Corporation, Troy, New York 12180-8349.
Virology. 1991 Mar;181(1):378-81. doi: 10.1016/0042-6822(91)90508-9.
Recently, we have reported the complete nucleotide sequence of vaccinia virus (Goebel, S. J., Johnson, G. P., Perkus, M. E., Davis, S. W., Winslow, J. P., and Paoletti, E. 1990, Virology 179, 247-266). Approximately 2.2 kbp leftward of the large subunit of ribonucleotide reductase resides a 108-amino acid open reading frame, O2L (nt 62,851-62,528) with significant similarity to known glutaredoxins. The deduced amino acid sequence of open reading frame O2L is 28.7% identical to the yeast and Escherichia coli proteins and greater than 40% identical to various mammalian glutaredoxins. Similar patterns of hydrophobicity as well as alpha-helix and beta-sheet potentials suggest that O2L and the glutaredoxins share a similar secondary structure. Furthermore, a common function is inferred by the presence of a highly conserved redox-active site.
最近，我们报道了痘苗病毒的完整核苷酸序列（戈贝尔，S.J.，约翰逊，G.P.，珀库斯，M.E.，戴维斯，S.W.，温斯洛，J.P.，和帕奥莱蒂，E.1990，《病毒学》179，247 - 266）。在核糖核苷酸还原酶大亚基向左约2.2千碱基对处，有一个108个氨基酸的开放阅读框O2L（核苷酸62,851 - 62,528），它与已知的谷氧还蛋白有显著相似性。开放阅读框O2L推导的氨基酸序列与酵母和大肠杆菌的蛋白质有28.7%的同一性，与各种哺乳动物谷氧还蛋白有超过40%的同一性。相似的疏水性模式以及α - 螺旋和β - 折叠潜能表明O2L和谷氧还蛋白共享相似的二级结构。此外，通过一个高度保守的氧化还原活性位点的存在推断出它们有共同的功能。
