Structural basis for contrasting activities of ribosome binding thiazole antibiotics.

@article{Lentzen2003StructuralBF,
  title={Structural basis for contrasting activities of ribosome binding thiazole antibiotics.},
  author={Georg Lentzen and Roscoe Klinck and Natalia Matassova and Fareed Aboul-Ela and Alastair I. H. Murchie},
  journal={Chemistry & biology},
  year={2003},
  volume={10 8},
  pages={769-78}
}
Thiostrepton and micrococcin inhibit protein synthesis by binding to the L11 binding domain (L11BD) of 23S ribosomal RNA. The two compounds are structurally related, yet they produce different effects on ribosomal RNA in footprinting experiments and on elongation factor-G (EF-G)-dependent GTP hydrolysis. Using NMR and an assay based on A1067 methylation by thiostrepton-resistance methyltransferase, we show that the related thiazoles, nosiheptide and siomycin, also bind to this region. The… CONTINUE READING

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