Abstract
A type II topoisomerase enzyme, DNA gyrase is responsible for catalysing the cleavage of double stranded DNA. It has been already demonstrated through detailed biochemical studies that fluoroquinolones potentially inhibit DNA resealing process by binding to cleaved sites of the DNA and gyrase enzyme. The present study makes use of a series of MD simulations to understand the complex biological interplay of DNA and the gyrase enzyme along with the fluoroquinolone molecule by reconstructing the broken backbone of DNA of Mtb DNA gyrase crystal structure complex. The molecular insights from the two series of molecular dynamics on cleaved and uncleaved DNA gyrase revealed many turns and twists into the molecular mechanism of fluoroquinolone drugs, which are presumably useful for the exploration of binary drug-enzyme complex and ternary enzyme-DNA-drug complex.
Published Version
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