title: Crystallization and preliminary crystallographic analysis of an aminoglycoside kinase from Legionella pneumophila.
abstract: 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 A.
authors.affiliation: Department of Microbiology and Immunology, McGill University, Canada.
authors.forename: Christopher T
authors.initials: CT
authors.lastname: Lemke
authors.forename: Jiyoung
authors.initials: J
authors.lastname: Hwang
authors.forename: Bing
authors.initials: B
authors.lastname: Xiong
authors.forename: Nicholas P
authors.initials: NP
authors.lastname: Cianciotto
authors.forename: Albert M
authors.initials: AM
authors.lastname: Berghuis
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003460:Crystallization / Q000379:methods; D019868:Kanamycin Kinase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D016952:Legionella pneumophila / Q000201:enzymology*; D016133:Polymerase Chain Reaction; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D019868:Kanamycin Kinase