Crystallization and preliminary crystallographic analysis of an aminoglycoside kinase from Legionella pneumophila
Journal Article
·
· Acta Crystallographica. Section F
- Department of Microbiology and Immunology, McGill University (Canada)
- Department of Biochemistry, McGill University (Canada)
- 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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