| Literature DB >> 18426901 |
Stéphanie Matrat1, Alexandra Aubry, Claudine Mayer, Vincent Jarlier, Emmanuelle Cambau.
Abstract
The replacement of M74 in GyrA, A83 in GyrA, and R447 in GyrB of Mycobacterium tuberculosis gyrase by their Escherichia coli homologs resulted in active enzymes as quinolone susceptible as the E. coli gyrase. This demonstrates that the primary structure of gyrase determines intrinsic quinolone resistance and was supported by a three-dimensional model of N-terminal GyrA.Entities:
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Year: 2008 PMID: 18426901 PMCID: PMC2493125 DOI: 10.1128/AAC.01380-07
Source DB: PubMed Journal: Antimicrob Agents Chemother ISSN: 0066-4804 Impact factor: 5.191