大肠杆菌核糖体蛋白L25的核磁共振结构显示出与一般应激蛋白和谷氨酰胺-tRNA合成酶的同源性。
The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases.
作者信息
Stoldt M, Wöhnert J, Görlach M, Brown L R
机构信息
Abteilung Molekulare Biophysik/NMR Spektroskopie, Institut für Molekulare Biotechnologie e. V., Postfach 100813, 07708 Jena, Germany.
出版信息
EMBO J. 1998 Nov 2;17(21):6377-84. doi: 10.1093/emboj/17.21.6377.
Abstract
The structure of the Escherichia coli ribosomal protein L25 has been determined to an r.m.s. displacement of backbone heavy atoms of 0.62 +/- 0.14 A by multi-dimensional heteronuclear NMR spectroscopy on protein samples uniformly labeled with 15N or 15N/13C. L25 shows a new topology for RNA-binding proteins consisting of a six-stranded beta-barrel and two alpha-helices. A putative RNA-binding surface for L25 has been obtained by comparison of backbone 15N chemical shifts for L25 with and without a bound cognate RNA containing the eubacterial E-loop that is the site for binding of L25 to 5S ribosomal RNA. Sequence comparisons with related proteins, including the general stress protein, CTC, show that the residues involved in RNA binding are highly conserved, thereby providing further confirmation of the binding surface. Tertiary structure comparisons indicate that the six-stranded beta-barrels of L25 and of the tRNA anticodon-binding domain of glutaminyl-tRNA synthetase are similar.
摘要
通过对用(^{15}N)或(^{15}N/^{13}C)均匀标记的蛋白质样品进行多维异核核磁共振光谱分析，已确定大肠杆菌核糖体蛋白L25的结构，其主链重原子的均方根位移为(0.62\pm0.14)埃。L25展示了一种新的RNA结合蛋白拓扑结构，由一个六链β桶和两个α螺旋组成。通过比较有和没有结合含有真细菌E环的同源RNA（E环是L25与5S核糖体RNA结合的位点）时L25的主链(^{15}N)化学位移，获得了L25的一个假定RNA结合表面。与相关蛋白（包括一般应激蛋白CTC）的序列比较表明，参与RNA结合的残基高度保守，从而进一步证实了该结合表面。三级结构比较表明，L25的六链β桶与谷氨酰胺-tRNA合成酶的tRNA反密码子结合结构域相似。
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