1RIP
RIBOSOMAL PROTEIN S17: CHARACTERIZATION OF THE THREE-DIMENSIONAL STRUCTURE BY 1H-AND 15N-NMR
Summary for 1RIP
| Entry DOI | 10.2210/pdb1rip/pdb |
| Descriptor | RIBOSOMAL PROTEIN S17 (1 entity in total) |
| Functional Keywords | ribosomal protein |
| Biological source | Geobacillus stearothermophilus |
| Total number of polymer chains | 1 |
| Total formula weight | 9555.31 |
| Authors | Golden, B.L.,Hoffman, D.W.,Ramakrishnan, V.,White, S.W. (deposition date: 1993-08-17, release date: 1993-10-31, Last modification date: 2024-05-22) |
| Primary citation | Golden, B.L.,Hoffman, D.W.,Ramakrishnan, V.,White, S.W. Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR. Biochemistry, 32:12812-12820, 1993 Cited by PubMed Abstract: 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. PubMed: 8251502DOI: 10.1021/bi00210a033 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
