A single point mutation in the DNA gyrase A protein greatly reduces binding of fluoroquinolones to the gyrase-DNA complex.
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.
Department of Biochemistry, University of Leicester, United Kingdom.
C J
CJ
Willmott
A
A
Maxwell
D000890:Anti-Infective Agents / Q000378:metabolism*; D004247:DNA / Q000187:drug effects / Q000378:metabolism*; D004250:DNA Topoisomerases, Type II / Q000235:genetics* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology; D009643:Norfloxacin / Q000378:metabolism; D017354:Point Mutation
D000890:Anti-Infective Agents; D004247:DNA; D004250:DNA Topoisomerases, Type II; D009643:Norfloxacin