Molecular recognition and modification of the 30S ribosome by the aminoglycoside-resistance methyltransferase NpmA.

@article{Dunkle2014MolecularRA,
  title={Molecular recognition and modification of the 30S ribosome by the aminoglycoside-resistance methyltransferase NpmA.},
  author={Jack A. Dunkle and Kellie Vinal and Pooja M Desai and Natalia Zelinskaya and Miloje Savic and Dayne M West and Graeme L. Conn and Christine M Dunham},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2014},
  volume={111 17},
  pages={
          6275-80
        }
}
Aminoglycosides are potent, broad spectrum, ribosome-targeting antibacterials whose clinical efficacy is seriously threatened by multiple resistance mechanisms. Here, we report the structural basis for 30S recognition by the novel plasmid-mediated aminoglycoside-resistance rRNA methyltransferase A (NpmA). These studies are supported by biochemical and functional assays that define the molecular features necessary for NpmA to catalyze m(1)A1408 modification and confer resistance. The requirement… CONTINUE READING
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Exogenously acquired 16S rRNA methyltransferases found in aminoglycoside-resistant pathogenic Gram-negative bacteria: an update.

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