1rip
From Proteopedia
|
RIBOSOMAL PROTEIN S17: CHARACTERIZATION OF THE THREE-DIMENSIONAL STRUCTURE BY 1H-AND 15N-NMR
Overview
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.
About this Structure
1RIP is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
Reference
Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR., Golden BL, Hoffman DW, Ramakrishnan V, White SW, Biochemistry. 1993 Nov 30;32(47):12812-20. PMID:8251502
Page seeded by OCA on Wed Nov 21 01:37:44 2007
