RIBOSOMAL PROTEIN-S17 - CHARACTERIZATION OF THE 3-DIMENSIONAL STRUCTURE BY H-1-NMR AND N-15-NMR

The structure of ribosomal protein S17 from Bacillus stearothermophilu s was investigated by two-dimensional homonuclear and heteronuclear ma gnetic resonance spectroscopy. The H-1 and N-15 chemical shift assignm ents are largely complete, and a preliminary structural characterizati on is presented. The protein consists of five beta-strands that form a single antiparallel beta-sheet with Greek-key topology. The beta-stra nds are connected by several extended loops, and two of these contain residue types that are frequently seen in the RNA-binding sites of pro teins. Additionally, two point mutations that affect antibiotic resist ance, translational fidelity, and ribosome assembly are located in the se 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.