Arrangement of Substrates at the Active Site of an Aminoglycoside Antibiotic 3‘-Phosphotransferase As Determined by NMR

The arrangements of the antibiotics amikacin and butirosin A at the active site of an aminoglycoside antibiotic 3‘-phosphotransferase (APH(3‘)-IIIa), which mediates resistance to a broad spectrum of aminoglycoside antibiotics, were determined. APH(3‘)-IIIa phosphorylates a wide range of aminoglycoside antibiotics in an ATP-dependent manner. β,γ-Bidentate CrATP, a stable exchange-inert metal−nucleotide analog, was used as a paramagnetic probe to …