Gibson T J, Argos P
European Molecular Biology Laboratory, Heidelberg, F.R.G.
J Mol Biol. 1990 Mar 5;212(1):7-9. doi: 10.1016/0022-2836(90)90298-Z.
The capsid protein of tomato bushy stunt virus (TBSV) has two antiparallel beta-sheet domains with the so-called jellyroll conformation. Contrary to previous analyses, we note that these domains are non-superimposable topologies. The TBSV shell (S) domain topology is common to many other proteins but the protruding (P) domain is a unique conformation so far found in no other protein. The TBSV capsid P domain did not arise from the S domain by a gene duplication event as previously assumed. It is proposed instead that the P domain was acquired from an as yet unidentified cellular protein. The four possible unique jellyroll topologies that might occur in proteins are discussed and illustrated.
番茄丛矮病毒(TBSV)的衣壳蛋白有两个具有所谓“果冻卷”构象的反平行β-折叠结构域。与之前的分析不同,我们注意到这些结构域具有不可重叠的拓扑结构。TBSV的外壳(S)结构域拓扑结构在许多其他蛋白质中很常见,但突出(P)结构域是迄今为止在其他蛋白质中未发现的独特构象。TBSV衣壳P结构域并非如之前所认为的那样通过基因复制事件从S结构域产生。相反,有人提出P结构域是从一种尚未鉴定的细胞蛋白中获得的。文中讨论并说明了蛋白质中可能出现的四种独特的果冻卷拓扑结构。