Modular structure of the full-length DNA gyrase B subunit revealed by small-angle X-ray scattering.

@article{Costenaro2007ModularSO,
  title={Modular structure of the full-length DNA gyrase B subunit revealed by small-angle X-ray scattering.},
  author={Lionel Costenaro and J. G{\"u}nter Grossmann and Christine Maria Isabel Ebel and Anthony Maxwell},
  journal={Structure},
  year={2007},
  volume={15 3},
  pages={329-39}
}
DNA gyrase, the only topoisomerase able to introduce negative supercoils into DNA, is essential for bacterial transcription and replication; absent from humans, it is a successful target for antibacterials. From biophysical experiments in solution, we report a structural model at approximately 12-15 A resolution of the full-length B subunit (GyrB). Analytical ultracentrifugation shows that GyrB is mainly a nonglobular monomer. Ab initio modeling of small-angle X-ray scattering data for GyrB… CONTINUE READING

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