Structural highlights
Function
[GYRB_ECO57] DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings.[HAMAP-Rule:MF_01898]
Publication Abstract from PubMed
Previously we have reported on a series of pyridine-3-carboxamide inhibitors of DNA gyrase and DNA topoisomerase IV that were designed using a computational de novo design approach and which showed promising antibacterial properties. Herein we describe the synthesis of additional examples from this series aimed specifically at DNA gyrase, along with crystal structures confirming the predicted mode of binding and in vitro ADME data which describe the drug-likeness of these compounds.
New insights into the binding mode of pyridine-3-carboxamide inhibitors of E. coli DNA gyrase.,Narramore S, Stevenson CEM, Maxwell A, Lawson DM, Fishwick CWG Bioorg Med Chem. 2019 Jun 14. pii: S0968-0896(19)30414-6. doi:, 10.1016/j.bmc.2019.06.015. PMID:31257079[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Narramore S, Stevenson CEM, Maxwell A, Lawson DM, Fishwick CWG. New insights into the binding mode of pyridine-3-carboxamide inhibitors of E. coli DNA gyrase. Bioorg Med Chem. 2019 Jun 14. pii: S0968-0896(19)30414-6. doi:, 10.1016/j.bmc.2019.06.015. PMID:31257079 doi:http://dx.doi.org/10.1016/j.bmc.2019.06.015
