TY - JOUR
T1 - Crystallization and preliminary crystallographic analysis of an aminoglycoside kinase from Legionella pneumophila
AU - Lemke, Christopher T.
AU - Hwang, Jiyoung
AU - Xiong, Bing
AU - Cianciotto, Nicholas P.
AU - Berghuis, Albert M.
PY - 2005
Y1 - 2005
N2 - 9-Aminoglycoside phosphotransferase type Ia [APH(9)-Ia] is a resistance factor in Legionella pneuemophila, the causative agent of legionnaires' disease. It is responsible for providing intrinsic resistance to the antibiotic spectinomycin. APH(9)-Ia phosphorylates one of the hydroxyl moieties of spectinomycin in an ATP-dependent manner, abolishing the antibiotic properties of this drug. Here, the crystallization and preliminary X-ray studies of this enzyme in two crystal forms is reported. One of the these crystal forms provides diffraction data to a resolution of 1.7 Å.
AB - 9-Aminoglycoside phosphotransferase type Ia [APH(9)-Ia] is a resistance factor in Legionella pneuemophila, the causative agent of legionnaires' disease. It is responsible for providing intrinsic resistance to the antibiotic spectinomycin. APH(9)-Ia phosphorylates one of the hydroxyl moieties of spectinomycin in an ATP-dependent manner, abolishing the antibiotic properties of this drug. Here, the crystallization and preliminary X-ray studies of this enzyme in two crystal forms is reported. One of the these crystal forms provides diffraction data to a resolution of 1.7 Å.
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U2 - 10.1107/S1744309105016301
DO - 10.1107/S1744309105016301
M3 - Article
C2 - 16511108
AN - SCOPUS:33744458715
SN - 1744-3091
VL - 61
SP - 606
EP - 608
JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
IS - 6
ER -