Structure and mechanism of DNA topoisomerase II

@article{Berger1996StructureAM,
  title={Structure and mechanism of DNA topoisomerase II},
  author={J. Berger and S. Gamblin and S. Harrison and JAMES C. Wang},
  journal={Nature},
  year={1996},
  volume={379},
  pages={225-232}
}
The crystal structure of a large fragment of yeast type II DNA topoisomerase reveals a heart-shaped dimeric protein with a large central hole. It provides a molecular model of the enzyme as an ATP-modulated clamp with two sets of jaws at opposite ends, connected by multiple joints. An enzyme with bound DNA can admit a second DNA duplex through one set of jaws, transport it through the cleaved first duplex, and expel it through the other set of jaws. 
DNA transport by a type II topoisomerase: direct evidence for a two-gate mechanism.
Type II DNA topoisomerases.
  • J. Berger
  • Biology, Medicine
  • Current opinion in structural biology
  • 1998
Structural insight into the quinolone–DNA cleavage complex of type IIA topoisomerases
Holoenzyme assembly and ATP-mediated conformational dynamics of topoisomerase VI
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