Structure of an Enzyme Required for Aminoglycoside Antibiotic Resistance Reveals Homology to Eukaryotic Protein Kinases

@article{Hon1997StructureOA,
  title={Structure of an Enzyme Required for Aminoglycoside Antibiotic Resistance Reveals Homology to Eukaryotic Protein Kinases},
  author={W. T. Hon and Geoffrey A. McKay and Paul Robert Thompson and Robert M. Sweet and Daniel S. Yang and Gerard D. Wright and Albert M Berghuis},
  journal={Cell},
  year={1997},
  volume={89},
  pages={887-895}
}
Bacterial resistance to aminoglycoside antibiotics is almost exclusively accomplished through either phosphorylation, adenylylation, or acetylation of the antibacterial agent. The aminoglycoside kinase, APH(3')-IIIa, catalyzes the phosphorylation of a broad spectrum of aminoglycoside antibiotics. The crystal structure of this enzyme complexed with ADP was determined at 2.2 A. resolution. The three-dimensional fold of APH(3')-IIIa reveals a striking similarity to eukaryotic protein kinases… CONTINUE READING
69 Citations
75 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 69 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 75 references

Catalytic mechanism of en - and substrate interactions

  • G. A. McKay, G. D. Wright
  • J . Biol . Chem .
  • 1996
Highly Influential
5 Excerpts

Kinetic mechanism of amino - plexed with an aminoglycoside antibiotic

  • G. A. McKay, G. D. Wright
  • Science
  • 1995
Highly Influential
5 Excerpts

Crystal structure of the tyrosine kinase domain of the human insulin receptor

  • S. R. Hubbard, L. Wei, L. Ellis, W. A. Hendrickson
  • Nature 372, 746–754.
  • 1994
Highly Influential
4 Excerpts

Similar Papers

Loading similar papers…