Article
Active-site residues of Escherichia coli DNA gyrase required in coupling ATP hydrolysis to DNA supercoiling and amino acid substitutions leading to novobiocin resistance.
Antimicrobial agents and chemotherapy - 1 Mar 2003
Gross Christian H, Parsons Jonathan D, Grossman Trudy H, Charifson Paul S, Bellon Steven, Jernee James, Dwyer Maureen, Chambers Stephen P, Markland William, Botfield Martyn, Raybuck Scott A
Abstract excerpt
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...
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