Structural highlights
Function
[C3SLN3_ECOLX] 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 (By similarity).[RuleBase:RU003363][HAMAP-Rule:MF_01898]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Bacterial DNA gyrase is an attractive target for the investigation of new antibacterial agents. Inhibitors of the GyrB subunit, which contains the ATP-binding site, are described in this communication. Novel, substituted 5-(1H-pyrazol-3-yl)thiazole compounds were identified as inhibitors of bacterial gyrase. Structure-guided optimization led to greater enzymatic potency and moderate antibacterial potency. Data are presented for the demonstration of selective enzyme inhibition of Escherichia coli GyrB over Staphylococcus aureus GyrB.
Discovery of pyrazolthiazoles as novel and potent inhibitors of bacterial gyrase.,Ronkin SM, Badia M, Bellon S, Grillot AL, Gross CH, Grossman TH, Mani N, Parsons JD, Stamos D, Trudeau M, Wei Y, Charifson PS Bioorg Med Chem Lett. 2010 May 1;20(9):2828-31. doi: 10.1016/j.bmcl.2010.03.052. , Epub 2010 Mar 15. PMID:20356737[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ronkin SM, Badia M, Bellon S, Grillot AL, Gross CH, Grossman TH, Mani N, Parsons JD, Stamos D, Trudeau M, Wei Y, Charifson PS. Discovery of pyrazolthiazoles as novel and potent inhibitors of bacterial gyrase. Bioorg Med Chem Lett. 2010 May 1;20(9):2828-31. doi: 10.1016/j.bmcl.2010.03.052. , Epub 2010 Mar 15. PMID:20356737 doi:10.1016/j.bmcl.2010.03.052
