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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Antitubercular Agents / pharmacology
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DNA Gyrase / chemistry
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DNA Gyrase / genetics*
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DNA Gyrase / metabolism*
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Drug Resistance, Bacterial / genetics
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Mycobacterium tuberculosis / drug effects*
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Mycobacterium tuberculosis / enzymology
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Mycobacterium tuberculosis / genetics
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Protein Structure, Secondary
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Quinolones / pharmacology*
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Sequence Homology, Amino Acid
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Structure-Activity Relationship
Substances
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Antitubercular Agents
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Quinolones
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DNA Gyrase