Open AccessCrystallization and preliminary crystallographic analysis of an aminoglycoside kinase from Legionella pneumophila
Author(s) -
Lemke Christopher T.,
Hwang Jiyoung,
Xiong Bing,
Cianciotto Nicholas P.,
Berghuis Albert M.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105016301
Subject(s) - legionella pneumophila , crystallization , phosphotransferase , legionnaires' disease , spectinomycin , aminoglycoside , chemistry , legionella , microbiology and biotechnology , antibiotics , crystal (programming language) , enzyme , crystallography , biochemistry , biology , antibiotic resistance , bacteria , organic chemistry , genetics , computer science , programming language
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.