Structural basis of quinolone inhibition of type IIA topoisomerases and target-mediated resistance

Wohlkonig, Alexandre, Chan, Pan F, Fosberry, Andrew P, Homes, Paul, Huang, Jianzhong, Kranz, Michael, Leydon, Vaughan R, Miles, Timothy J, Pearson, Neil D, Perera, Rajika L, Shillings, Anthony J, Gwynn, Michael N and Bax, Benjamin D ORCID: https://orcid.org/0000-0003-1940-3785 2010. Structural basis of quinolone inhibition of type IIA topoisomerases and target-mediated resistance. Nature Structural and Molecular Biology 17 (99) , pp. 1152-1153. 10.1038/nsmb.1892

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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

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Publisher:	Nature Publishing Group
ISSN:	1545-9993
Date of Acceptance:	15 July 2010
Last Modified:	23 Oct 2022 14:03
URI:	https://orca.cardiff.ac.uk/id/eprint/112629

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