Structural analyses of nucleotide binding to an aminoglycoside phosphotransferase.

@article{Burk2001StructuralAO,
  title={Structural analyses of nucleotide binding to an aminoglycoside phosphotransferase.},
  author={David L. Burk and W. C. Hon and Adam K C Leung and Albert M Berghuis},
  journal={Biochemistry},
  year={2001},
  volume={40 30},
  pages={8756-64}
}
3',5"-Aminoglycoside phosphotransferase type IIIa [APH(3')-IIIa] is a bacterial enzyme that confers resistance to a range of aminoglycoside antibiotics while exhibiting striking homology to eukaryotic protein kinases (ePK). The structures of APH(3')-IIIa in its apoenzyme form and in complex with the nonhydrolyzable ATP analogue AMPPNP were determined to 3.2 and 2.4 A resolution, respectively. Furthermore, refinement of the previously determined ADP complex was completed. The structure of the… CONTINUE READING

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