Wilson K S, Appelt K, Badger J, Tanaka I, White S W
Proc Natl Acad Sci U S A. 1986 Oct;83(19):7251-5. doi: 10.1073/pnas.83.19.7251.
The structure of ribosomal protein L30 from Bacillus stearothermophilus has been solved to a resolution of 2.5 A. The molecule is somewhat elongated and contains two helices and a three-stranded, anti-parallel beta-pleated sheet. The protein fold, in which helices pack on the same side of the sheet, generates a simple helix-sheet, two-layered motif. It is possible to distinguish three hydrophobic patches on the molecular surface, and one end has six isolated arginine and lysine residues. It is proposed that these reflect sites of protein-protein and protein-RNA interaction, respectively. The protein fold is very similar to that of the only other known ribosomal protein structure, L7/L12 from Escherichia coli, and, based on this similarity, an attempt is made to align the amino acid sequences of the two proteins.
嗜热脂肪芽孢杆菌核糖体蛋白L30的结构已解析至2.5埃的分辨率。该分子略显细长，包含两个螺旋和一个三股反平行β折叠片层。蛋白质折叠中，螺旋堆积在片层的同一侧，形成了一个简单的螺旋-片层两层基序。在分子表面可以区分出三个疏水斑块，一端有六个孤立的精氨酸和赖氨酸残基。据推测，这些分别反映了蛋白质-蛋白质和蛋白质-RNA相互作用的位点。该蛋白质折叠与另一种已知的核糖体蛋白结构——大肠杆菌的L7/L12非常相似，并基于这种相似性尝试对这两种蛋白质的氨基酸序列进行比对。
