title: Flipping the Switch "On" for Aminoglycoside-Resistance Enzymes: The Mechanism Is Finally Revealed!
abstract: In a recent issue of Structure, Caldwell et al. (2016) determined crystal structures of APH(2″)-Ia in complex with various combinations of aminoglycosides and nucleosides, which compellingly revealed that the catalytic activity of this resistance enzyme is regulated by a conformational change of the triphosphate of GTP, a mechanism previously unknown for antibiotic kinases.
authors.affiliation: Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536-0596, USA.
authors.forename: Huy X
authors.initials: HX
authors.lastname: Ngo
authors.affiliation: Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536-0596, USA. Electronic address: sylviegtsodikova@uky.edu.
authors.forename: Sylvie
authors.initials: S
authors.lastname: Garneau-Tsodikova
mesh_terms: D000617:Aminoglycosides; D000900:Anti-Bacterial Agents; D019868:Kanamycin Kinase / Q000737:chemistry*; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000737:chemistry
chemical_list: D000617:Aminoglycosides; D000900:Anti-Bacterial Agents; D017853:Phosphotransferases (Alcohol Group Acceptor); D019868:Kanamycin Kinase