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Default Ribosomal protein S17: characterization of the three-dimensional structure by 1H and

Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR.

Related Articles Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR.

Biochemistry. 1993 Nov 30;32(47):12812-20

Authors: Golden BL, Hoffman DW, Ramakrishnan V, White SW

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.

PMID: 8251502 [PubMed - indexed for MEDLINE]



Source: PubMed
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