Mutagenesis in the α3α4 GyrA Helix and in the Toprim Domain of GyrB Refines the Contribution of Mycobacterium tuberculosis DNA Gyrase to Intrinsic Resistance to Quinolones
2008 ◽
Vol 52
(8)
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pp. 2909-2914
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Keyword(s):
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.
1991 ◽
Vol 221
(1)
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pp. 293-308
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Keyword(s):
1999 ◽
Vol 37
(1)
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pp. 130-143
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Keyword(s):
2013 ◽
Vol 425
(14)
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pp. 2591-2608
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1994 ◽
Vol 236
(2)
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pp. 618-628
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Keyword(s):
2020 ◽
Keyword(s):
1986 ◽
Vol 48
(2)
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pp. 67-101
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1996 ◽
Vol 242
(2)
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pp. 235-242
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