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Research Article

A single point mutation in the DNA gyrase A protein greatly reduces binding of fluoroquinolones to the gyrase-DNA complex.

C J Willmott, A Maxwell
C J Willmott
Department of Biochemistry, University of Leicester, United Kingdom.
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A Maxwell
Department of Biochemistry, University of Leicester, United Kingdom.
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DOI: 10.1128/AAC.37.1.126
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ABSTRACT

Binding of the quinolone drug norfloxacin to gyrase and DNA has been investigated. We have detected binding to gyrase-DNA complex but find no significant binding to either gyrase or DNA alone. Enzyme containing gyrase A protein with the mutation Ser-83 to Trp (conferring quinolone resistance) showed greatly reduced drug binding.

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A single point mutation in the DNA gyrase A protein greatly reduces binding of fluoroquinolones to the gyrase-DNA complex.
C J Willmott, A Maxwell
Antimicrobial Agents and Chemotherapy Jan 1993, 37 (1) 126-127; DOI: 10.1128/AAC.37.1.126

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A single point mutation in the DNA gyrase A protein greatly reduces binding of fluoroquinolones to the gyrase-DNA complex.
C J Willmott, A Maxwell
Antimicrobial Agents and Chemotherapy Jan 1993, 37 (1) 126-127; DOI: 10.1128/AAC.37.1.126
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