Abstracting and Indexing

  • Google Scholar
  • CrossRef
  • WorldCat
  • ResearchGate
  • Scilit
  • DRJI
  • Semantic Scholar
  • Academic Keys
  • Microsoft Academic
  • Academia.edu
  • Baidu Scholar
  • Scribd

Structure Based Insights into the Association of Fluoroquinolones with Mycobacterial DNA-Gyrase Complexes

Author(s): Siva Kumar G, Harmanpreet singh, Elizabeth Sobhia M

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.

Journal Statistics

Impact Factor: * 4.2

CiteScore: 2.9

Acceptance Rate: 11.01%

Time to first decision: 10.4 days

Time from article received to acceptance: 2-3 weeks

Discover More: Recent Articles

Grant Support Articles

© 2016-2024, Copyrights Fortune Journals. All Rights Reserved!