EC Number   |
|---|
   2.3.2.12 | - |
| 2.3.2.12 | cross-crystal averaging over two crystal structures of the 70S ribosome in the same functional state. The structure of the peptidyl transferase center is the same in the functionally equivalent 70S ribosome and the 50S subunit |
| 2.3.2.12 | hanging drop vapor diffusion method, using 85 mM sodium citrate, pH 5.6, 25.5% (w/v) polyethylene glycol 4000, 170 mM ammonium acetate, and 15% (v/v) glycerol |
| 2.3.2.12 | sitting drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M bis-Tris-HCl pH 6.5, 25% (w/v) PEG 3350 |
| 2.3.2.12 | structure of the inhibitor linezolid bound to the 50S ribosomal subunit. Linezolid binds in the A site pocket at the peptidyltransferase center of the ribosome overlapping the aminoacyl moiety of an A-site bound tRNA as well as many clinically important antibiotics. Binding of linezolid stabilizes a distinct conformation of the universally conserved 23S rRNA nucleotide U2585 that would be nonproductive for peptide bond formation. In a model oxazolidinones impart their inhibitory effect by perturbing the correct positioning of tRNAs on the ribosome |
| 2.3.2.12 | structures at 3.5 A and 3.55 A resolution of the 70S ribosome in complex with A- and P-site tRNAs that mimic pre- and postpeptidyl transfer states, respectively. The peptidyl transfer center is very similar between the 50S subunit and the intact ribosome. Structures reveal interactions between ribosomal proteins L16 and L27 and the tRNA substrates |
| 2.3.2.12 | Thermus thermophilus 70S ribosomes complexed with mRNA and P-site (fMet-tRNAifMet) and A-site (Phe-tRNAPhe) substrates, co-crystallization of inhibitor madumycin II, sitting drop vapor diffusion method, 70S ribosome complexes are formed in buffer containing 5 mM HEPES-KOH, pH 7.6, 50 mM KCl, 10 mM NH4Cl, and 10 mM Mg(CH3COO)2, and then crystallized in buffer containing 100 mM Tris-HCl, pH 7.6, 2.9% w/v PEG 20000, 7-12% v/v MPD, 100-200 mM arginine, 0.5 mM 2-mercaptoethanol, 19°C, X-ray diffraction structure determination and analysis at 2.8 A resolution, molecular replacement, structure modeling |
