Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomerase.

@article{Wei2005NucleotidedependentDM,
  title={Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomerase.},
  author={Hua Wei and Alexander J Ruthenburg and Seth K. Bechis and Gregory L. Verdine},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 44},
  pages={37041-7}
}
Type IIA DNA topoisomerases play multiple essential roles in the management of higher-order DNA structure, including modulation of topological state, chromosome segregation, and chromatin condensation. These diverse physiologic functions are all accomplished through a common molecular mechanism, wherein the protein catalyzes transient cleavage of a DNA duplex (the G-segment) to yield a double-stranded gap through which another duplex (the T-segment) is passed. The overall process is… CONTINUE READING

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