A crystal structure of the bifunctional antibiotic simocyclinone D8, bound to DNA gyrase.

@article{Edwards2009ACS,
  title={A crystal structure of the bifunctional antibiotic simocyclinone D8, bound to DNA gyrase.},
  author={Marcus J. Edwards and Ruth H Flatman and Lesley A. Mitchenall and Clare Elizabeth Mary Stevenson and Tung B K Le and Thomas A Clarke and Adam R. McKay and H. -P. Fiedler and Mark J. Buttner and David M. Lawson and Anthony Maxwell},
  journal={Science},
  year={2009},
  volume={326 5958},
  pages={1415-8}
}
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… CONTINUE READING

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Pharmazie in unserer Zeit • 2010
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Proceedings of the National Academy of Sciences of the United States of America • 2014

New aminocoumarin antibiotics as gyrase inhibitors.

International journal of medical microbiology : IJMM • 2014

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