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

Chris Willmott | Zendy; Anthony Maxwell | Zendy

Open Access

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

Author(s) -

Chris Willmott,

Anthony Maxwell

Publication year - 1993

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.37.1.126

Subject(s) - dna gyrase , norfloxacin , dna , quinolone , point mutation , binding site , biology , biochemistry , mutation , chemistry , microbiology and biotechnology , escherichia coli , gene , antibiotics , ciprofloxacin

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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