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Crystallization and preliminary crystallographic analysis of an aminoglycoside kinase from Legionella pneumophila

Journal Article · · Acta Crystallographica. Section F
 [1];  [2];  [1];  [3]
  1. Department of Microbiology and Immunology, McGill University (Canada)
  2. Department of Biochemistry, McGill University (Canada)
  3. Department of Microbiology and Immunology, Northwestern University (United States)

Two crystal forms of the antibiotic resistance enzyme APH(9)-Ia from L. pneumophila are reported. 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.

OSTI ID:
22356033
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 6 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English

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