RIBOSOMAL PROTEIN-S17 - CHARACTERIZATION OF THE 3-DIMENSIONAL STRUCTURE BY H-1-NMR AND N-15-NMR
RIBOSOMAL PROTEIN-S17 - CHARACTERIZATION OF THE 3-DIMENSIONAL STRUCTURE BY H-1-NMR AND N-15-NMR
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DOI：
10.1021/bi00210a033
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发表时间：
1993-11-30
期刊：
影响因子：
2.9
通讯作者：
WHITE, SW
中科院分区：
文献类型：
--
作者：
GOLDEN, BL;HOFFMAN, DW;WHITE, SW
对嗜热脂肪芽孢杆菌核糖体蛋白S17进行了二维同核和异核磁共振波谱研究。H-1和N-15的化学位移指定已基本完成，并给出了初步的结构表征。该蛋白质由五条β-链组成，它们形成一个具有希腊键拓扑结构的反平行的β-折叠。β链由几个延伸的环连接，其中两个环含有蛋白质RNA结合位点中常见的残基类型。此外，影响抗生素耐药性、翻译保真度和核糖体组装的两个点突变位于蛋白质的这两个区域。由于这些潜在的RNA结合位点分布在蛋白质的大表面上，因此该分子似乎可能与16S rRNA的几个区域相互作用。
The structure of ribosomal protein S17 from Bacillus stearothermophilus was investigated by two-dimensional homonuclear and heteronuclear magnetic resonance spectroscopy. The H-1 and N-15 chemical shift assignments are largely complete, and a preliminary structural characterization is presented. The protein consists of five beta-strands that form a single antiparallel beta-sheet with Greek-key topology. The beta-strands are connected by several extended loops, and two of these contain residue types that are frequently seen in the RNA-binding sites of proteins. Additionally, two point mutations that affect antibiotic resistance, translational fidelity, and ribosome assembly are located in these two regions of the protein. Since these potential RNA-binding sites are distributed over a large surface of the protein, it appears that the molecule may interact with several regions of 16S rRNA.