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 A. Ruthenburg and S. Bechis and G. Verdine},
  journal={Journal of Biological Chemistry},
  year={2005},
  volume={280},
  pages={37041 - 37047}
}
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… Expand
Trapping of the transport-segment DNA by the ATPase domains of a type II topoisomerase
Holoenzyme assembly and ATP-mediated conformational dynamics of topoisomerase VI
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