The Interaction of Drugs with DNA Gyrase: A Model for the Molecular Basis of Quinolone Action
| Autor: | Faye M. Barnard, Anthony Maxwell, Lois M. Wentzell, Jonathan G. Heddle |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Macromolecular Substances
Protein Conformation medicine.drug_class Molecular Conformation Quinolones Biochemistry DNA gyrase Structure-Activity Relationship chemistry.chemical_compound Protein structure Anti-Infective Agents Bacterial Proteins Coumarins Genetics medicine Humans Topoisomerase II Inhibitors heterocyclic compounds Enzyme Inhibitors Binding site Polymerase Binding Sites Bacteria biology Chemistry DNA General Medicine Quinolone Protein Structure Tertiary Protein Subunits Models Chemical biology.protein Molecular Medicine DNA supercoil Topoisomerase-II Inhibitor Novobiocin |
| Zdroj: | Nucleosides, Nucleotides and Nucleic Acids. 19:1249-1264 |
| ISSN: | 1532-2335 1525-7770 |
| Popis: | DNA gyrase supercoils DNA in bacteria. The fact that it is essential in all bacteria and absent from eukaryotes makes it an ideal drug target. We discuss the action of coumarin and quinolone drugs on gyrase. In the case of coumarins, the drugs are known to be competitive inhibitors of the gyrase ATPase reaction. From a combination of structural and biochemical studies, the molecular details of the gyrase-coumarin complex are well established. In the case of quinolones, the drugs are thought to act by stabilising a cleavage complex between gyrase and DNA that arrests polymerases in vivo. The exact nature of the gyrase-quinolone-DNA complex is not known; we propose a model for this complex based on structural and biochemical data. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|