Structural basis of quinolone inhibition of type IIA topoisomerases and target-mediated resistance.
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Wohlkonig A, Chan PF, Fosberry AP, Homes P, Huang J, Kranz M, Leydon VR, Miles TJ, Pearson ND, Perera RL, Shillings AJ, Gwynn MN, Bax BD
Structural basis of quinolone inhibition of type IIA topoisomerases and target-mediated resistance.
Nat Struct Mol Biol. 2010 Sep;17(9):1152-3. doi: 10.1038/nsmb.1892. Epub 2010 Aug 29.
- PubMed ID
- 20802486 [ View in PubMed]
- Abstract
Quinolone antibacterials have been used to treat bacterial infections for over 40 years. A crystal structure of moxifloxacin in complex with Acinetobacter baumannii topoisomerase IV now shows the wedge-shaped quinolone stacking between base pairs at the DNA cleavage site and binding conserved residues in the DNA cleavage domain through chelation of a noncatalytic magnesium ion. This provides a molecular basis for the quinolone inhibition mechanism, resistance mutations and invariant quinolone antibacterial structural features.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Moxifloxacin DNA topoisomerase 2-alpha Protein Humans UnknownInhibitorDetails