Active-site residues of Escherichia coli DNA gyrase required in coupling ATP hydrolysis to DNA supercoiling and amino acid substitutions leading to novobiocin resistance.

@article{Gross2003ActivesiteRO,
  title={Active-site residues of Escherichia coli DNA gyrase required in coupling ATP hydrolysis to DNA supercoiling and amino acid substitutions leading to novobiocin resistance.},
  author={Christian H Gross and Jonathan D Parsons and Trudy H. Grossman and Paul S. Charifson and Steven F. Bellon and James Jernee and Maureen Dwyer and Stephen P. Chambers and William Markland and Martyn C Botfield and Scott A. Raybuck},
  journal={Antimicrobial agents and chemotherapy},
  year={2003},
  volume={47 3},
  pages={1037-46}
}
DNA gyrase is a bacterial type II topoisomerase which couples the free energy of ATP hydrolysis to the introduction of negative supercoils into DNA. Amino acids in proximity to bound nonhydrolyzable ATP analog (AMP. PNP) or novobiocin in the gyrase B (GyrB) subunit crystal structures were examined for their roles in enzyme function and novobiocin resistance by site-directed mutagenesis. Purified Escherichia coli GyrB mutant proteins were complexed with the gyrase A subunit to form the… CONTINUE READING