NMR structural characterization of the N-terminal active domain of the gyrase B subunit from Pseudomonas aeruginosa and its complex with an inhibitor

FEBS Letters(2015)

Cited 13|Views15
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Abstract
•The bis-pyridylurea inhibitor improved NMR spectra of pGyrB.•The inhibitor binds to pGyrB with a binding constant of 54.6nM.•Backbone assignments of both free and inhibitor bound pGyrB were obtained.•The Inhibitor did not alter pGyrB structure.•The inhibitor binds to ATP binding pocket.
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Key words
NMR,Drug discovery,Topoisomerase,Gyrase B,Structure-based drug design
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