Crystal structure of the breakage–reunion domain of DNA gyrase

@article{Cabral1997CrystalSO,
  title={Crystal structure of the breakage–reunion domain of DNA gyrase},
  author={J. Cabral and A. P. Jackson and Clare V. Smith and N. Shikotra and A. Maxwell and R. Liddington},
  journal={Nature},
  year={1997},
  volume={388},
  pages={903-906}
}
DNA gyrase is a type II DNA topoisomerase from bacteria that introduces supercoils into DNA,. It catalyses the breakage of a DNA duplex (the G segment), the passage of another segment (the T segment) through the break, and then the reunification of the break. This activity involves the opening and closing of a series of molecular ‘gates’ which is coupled to ATP hydrolysis. Here we present the crystal structure of the ‘breakage–reunion’ domain of the gyrase at 2.8 Å resolution. Comparison of the… Expand
Crystal structure of DNA gyrase B′ domain sheds lights on the mechanism for T-segment navigation
DNA Topoisome Trapping a DNA in Motion
Solution structures of DNA-bound gyrase
Cryo-EM structure of the complete E. coli DNA Gyrase nucleoprotein complex
DNA Topoisomerase Inhibitors: Trapping a DNA-Cleaving Machine in Motion
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 21 REFERENCES
Conversion of DNA gyrase into a conventional type II topoisomerase.
  • S. Kampranis, A. Maxwell
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1996
DNA gyrase: structure and function.
  • R. Reece, A. Maxwell
  • Biology, Medicine
  • Critical reviews in biochemistry and molecular biology
  • 1991
DNA transport by a type II DNA topoisomerase: Evidence in favor of a two-gate mechanism
DNA transport by a type II topoisomerase: direct evidence for a two-gate mechanism.
Neutron and light-scattering studies of DNA gyrase and its complex with DNA.
On the coupling between ATP usage and DNA transport by yeast DNA topoisomerase II.
...
1
2
3
...