2y3p

CRYSTAL STRUCTURE OF N-TERMINAL DOMAIN OF GYRA WITH THE ANTIBIOTIC SIMOCYCLINONE D8

spinqualitylabelsall models 2y3p, resolution 2.62Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2y3p is a 2 chain structure with sequence from Escherichia coli. This structure supersedes the now removed PDB entry 2wl2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG, SM8 Activity: DNA topoisomerase (ATP-hydrolyzing), with EC number 5.99.1.3 Resources: FirstGlance, OCA, RCSB, PDBsum Function [GYRA_SHIFL] 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). Publication Abstract from PubMed Simocyclinones are bifunctional antibiotics that inhibit bacterial DNA gyrase by preventing DNA binding to the enzyme. We report the crystal structure of the complex formed between the N-terminal domain of the Escherichia coli gyrase A subunit and simocyclinone D8, revealing two binding pockets that separately accommodate the aminocoumarin and polyketide moieties of the antibiotic. These are close to, but distinct from, the quinolone-binding site, consistent with our observations that several mutations in this region confer resistance to both agents. Biochemical studies show that the individual moieties of simocyclinone D8 are comparatively weak inhibitors of gyrase relative to the parent compound, but their combination generates a more potent inhibitor. Our results should facilitate the design of drug molecules that target these unexploited binding pockets. A crystal structure of the bifunctional antibiotic simocyclinone D8, bound to DNA gyrase.,Edwards MJ, Flatman RH, Mitchenall LA, Stevenson CE, Le TB, Clarke TA, McKay AR, Fiedler HP, Buttner MJ, Lawson DM, Maxwell A Science. 2009 Dec 4;326(5958):1415-8. PMID:19965760 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Gyrase

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