Substrate Recognition and Modification by the Nosiheptide Resistance Methyltransferase

@inproceedings{Yin2015SubstrateRA,
  title={Substrate Recognition and Modification by the Nosiheptide Resistance Methyltransferase},
  author={Sitao Yin and Hengyi Jiang and Dongrong Chen and Alastair I. H. Murchie},
  booktitle={PloS one},
  year={2015}
}
BACKGROUND The proliferation of antibiotic resistant pathogens is an increasing threat to the general public. Resistance may be conferred by a number of mechanisms including covalent or mutational modification of the antibiotic binding site, covalent modification of the drug, or the over-expression of efflux pumps. The nosiheptide resistance methyltransferase (NHR) confers resistance to the thiazole antibiotic nosiheptide in the nosiheptide producer organism Streptomyces actuosus through 2'O… CONTINUE READING

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Although the crystal structures of NHR and the closely related thiostrepton - resistance methyltransferase ( TSR ) in complex with the cofactor S - Adenosyl - L - methionine ( SAM ) are available , the principles behind NHR substrate recognition and catalysis remain unclear .
Although the crystal structures of NHR and the closely related thiostrepton - resistance methyltransferase ( TSR ) in complex with the cofactor S - Adenosyl - L - methionine ( SAM ) are available , the principles behind NHR substrate recognition and catalysis remain unclear .
Although the crystal structures of NHR and the closely related thiostrepton - resistance methyltransferase ( TSR ) in complex with the cofactor S - Adenosyl - L - methionine ( SAM ) are available , the principles behind NHR substrate recognition and catalysis remain unclear .
Although the crystal structures of NHR and the closely related thiostrepton - resistance methyltransferase ( TSR ) in complex with the cofactor S - Adenosyl - L - methionine ( SAM ) are available , the principles behind NHR substrate recognition and catalysis remain unclear .
Although the crystal structures of NHR and the closely related thiostrepton - resistance methyltransferase ( TSR ) in complex with the cofactor S - Adenosyl - L - methionine ( SAM ) are available , the principles behind NHR substrate recognition and catalysis remain unclear .
Although the crystal structures of NHR and the closely related thiostrepton - resistance methyltransferase ( TSR ) in complex with the cofactor S - Adenosyl - L - methionine ( SAM ) are available , the principles behind NHR substrate recognition and catalysis remain unclear .
The nosiheptide resistance methyltransferase ( NHR ) confers resistance to the thiazole antibiotic nosiheptide in the nosiheptide producer organism Streptomyces actuosus through 2'O - methylation of 23S rRNA at the nucleotide A1067 .
The nosiheptide resistance methyltransferase ( NHR ) confers resistance to the thiazole antibiotic nosiheptide in the nosiheptide producer organism Streptomyces actuosus through 2'O - methylation of 23S rRNA at the nucleotide A1067 .
The nosiheptide resistance methyltransferase ( NHR ) confers resistance to the thiazole antibiotic nosiheptide in the nosiheptide producer organism Streptomyces actuosus through 2'O - methylation of 23S rRNA at the nucleotide A1067 .
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