The high-resolution crystal structure of a 24-kDa gyrase B fragment from E. coli complexed with one of the most potent coumarin inhibitors, clorobiocin.

@article{Tsai1997TheHC,
  title={The high-resolution crystal structure of a 24-kDa gyrase B fragment from E. coli complexed with one of the most potent coumarin inhibitors, clorobiocin.},
  author={Francis T.F. Tsai and Okram Mukherjee Singh and Tadeusz J Skarzynski and Alan J. Wonacott and Steve Weston and Alan Tucker and Richard A. Pauptit and A L Breeze and John Poyser and Ronan O'Brien and John E. Ladbury and Dale B. Wigley},
  journal={Proteins},
  year={1997},
  volume={28 1},
  pages={41-52}
}
Coumarin antibiotics, such as clorobiocin, novobiocin, and coumermycin A1, inhibit the supercoiling activity of gyrase by binding to the gyrase B (GyrB) subunit. Previous crystallographic studies of a 24-kDa N-terminal domain of GyrB from E. coli complexed with novobiocin and a cyclothialidine analogue have shown that both ligands act by binding at the ATP-binding site. Clorobiocin is a natural antibiotic isolated from several Streptomyces strains and differs from novobiocin in that the methyl… CONTINUE READING
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