Structural Basis for DNA Gyrase Interaction with Coumermycin A1
نویسندگان
چکیده
منابع مشابه
Novobiocin and coumermycin inhibit DNA supercoiling catalyzed by DNA gyrase.
Novobiocin and coumermycin are known to inhibit the replication of DNA iing of DNA catalyzed by E. coli DNA gyrase, a recently discovered enzyme that introduces negative superhelical turns into covalently circular DNA. The activity of DNA gyrase purified from a coumermycin-resistant mutant strain is resistant to both drugs. The inhibition by novobiocin of colicin E1 plasmid DNA replication in a...
متن کاملSite-specific interaction of DNA gyrase with DNA.
DNA gyrase, in the presence of the inhibitor oxolinic acid, can induce double-strand DNA breakage at specific sites. The sequences at several sites have been determined. In addition, the structure of complexes formed between DNA gyrase and restriction fragments containing an oxolinic acid-promoted cleavage site has been examined by DNase protection methods. DNA gyrase protects more than 120 bas...
متن کاملCoumermycin A1 inhibits growth and induces relaxation of supercoiled plasmids in Borrelia burgdorferi, the Lyme disease agent.
Coumermycin A1 is an inhibitor of DNA gyrase, an enzyme that catalyzes supercoiling of DNA and is required for bacterial DNA replication. We have investigated the activity of this coumarin antibiotic on Borrelia burgdorferi, a spirochete and the causative agent of Lyme disease. B. burgdorferi was more susceptible than many other eubacteria to coumermycin as well as novobiocin, another coumarin ...
متن کاملStructural Basis for Cooperative DNA
when the bacterial environment contains no lactose (Al-berts et al., 2002; Berg et al., 2002). The repressor functions as a dimer of two " hand " domains (Figure 1D). loop is critical for the lac operon repression (Matthews, 1992). The primary roles of CAP and LR are the opposite of Summary each other, yet the two proteins bind to DNA cooperatively (Hudson and Fried, 1990; Lewis et al., 1996). ...
متن کاملStructural basis of DNA gyrase inhibition by antibacterial QPT-1, anticancer drug etoposide and moxifloxacin
New antibacterials are needed to tackle antibiotic-resistant bacteria. Type IIA topoisomerases (topo2As), the targets of fluoroquinolones, regulate DNA topology by creating transient double-strand DNA breaks. Here we report the first co-crystal structures of the antibacterial QPT-1 and the anticancer drug etoposide with Staphylococcus aureus DNA gyrase, showing binding at the same sites in the ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Medicinal Chemistry
سال: 2019
ISSN: 0022-2623,1520-4804
DOI: 10.1021/acs.jmedchem.8b01928