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

by Wohlkonig, Alexandre , Bax, Benjamin D , Fosberry, Andrew P , Gwynn, Michael N , Shillings, Anthony J , Kranz, Michael , Leydon, Vaughan R , Miles, Timothy J , Huang, Jianzhong , Pearson, Neil D , Homes, Paul , Chan, Pan F , Perera, Rajika L

in 631/326/252/22/1290 / 631/45/535 / 631/45/607/1165 / 631/92/609 / Acinetobacter baumannii / Acinetobacter baumannii - enzymology / Bacteria / Bacterial diseases / Bacterial infections / Biochemistry / Biological Microscopy / Biomedical and Life Sciences / brief-communication / Chelation / Chemical properties / Crystal structure / Deoxyribonucleic acid / DNA / DNA Topoisomerase IV - chemistry / DNA Topoisomerase IV - pharmacology / Drug resistance / Drug therapy / Enzyme Inhibitors - chemistry / Enzyme Inhibitors - pharmacology / Genetic aspects / Life Sciences / Magnesium / Membrane Biology / Microbial drug resistance / Models, Molecular / Moxifloxacin / Mutation / Protein Structure / Protein Structure, Quaternary / Protein Structure, Tertiary / Quinolones - chemistry / Quinolones - pharmacology / Structure / Topoisomerases

2010

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

2010

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

2010

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Journal Article

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

Wohlkonig, Alexandre,

Bax, Benjamin D,

Fosberry, Andrew P,

Gwynn, Michael N,

Shillings, Anthony J,

Kranz, Michael,

Leydon, Vaughan R,

Miles, Timothy J,

Huang, Jianzhong,

Pearson, Neil D,

Homes, Paul,

Chan, Pan F,

Perera, Rajika L

2010

Overview

The structure of Moxifloxacin, a quinolone antibacterial, in complex with Acinetobacter baumannii topoisomerase IV and DNA now shows how the drug stacks between base pairs at the DNA cleavage site. Moxifloxacin contacts the protein through a non-catalytic Mg 2+ , and the structure gives insight into the mode of inhibition and possible basis of drug resistance. 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.

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Publisher

Nature Publishing Group US,Nature Publishing Group

Subject

/ Acinetobacter baumannii

/ Acinetobacter baumannii - enzymology

/ Bacteria