Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR.
The structure of ribosomal protein S17 from Bacillus stearothermophilus was investigated by two-dimensional homonuclear and heteronuclear magnetic resonance spectroscopy. The 1H and 15N 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.
Golden
B L
BL
Department of Microbiology, Duke University Medical Center, Durham, North Carolina 27710.
Hoffman
D W
DW
Ramakrishnan
V
V
White
S W
SW
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D005798:Genes, Bacterial; D001411:Geobacillus stearothermophilus / Q000737:chemistry* / Q000235:genetics; D006859:Hydrogen / Q000737:chemistry; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009584:Nitrogen / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D011994:Recombinant Proteins; D012269:Ribosomal Proteins; C037084:ribosomal protein S17; D006859:Hydrogen; D009584:Nitrogen