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

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. Th...

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Veröffentlicht in:	Cell 1997-06, Vol.89 (6), p.887-895
Hauptverfasser:	Hon, Wai-Ching, McKay, Geoffrey A., Thompson, Paul R., Sweet, Robert M., Yang, Daniel S.C., Wright, Gerard D., Berghuis, Albert M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Aminoglycosides Anti-Bacterial Agents Binding Sites - physiology Crystallography Drug Resistance, Microbial Enterococcus - chemistry Enterococcus - enzymology Enterococcus - genetics Eukaryotic Cells - enzymology Kanamycin Kinase Molecular Sequence Data Phosphotransferases (Alcohol Group Acceptor) - chemistry Phosphotransferases (Alcohol Group Acceptor) - genetics Phosphotransferases (Alcohol Group Acceptor) - metabolism Protein Kinases - chemistry Protein Kinases - genetics Protein Structure, Secondary Protein Structure, Tertiary Sequence Homology, Amino Acid Signal Transduction - physiology Staphylococcus - chemistry Staphylococcus - enzymology Staphylococcus - genetics
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