Holoenzyme assembly and ATP-mediated conformational dynamics of topoisomerase VI

@article{Corbett2007HoloenzymeAA,
  title={Holoenzyme assembly and ATP-mediated conformational dynamics of topoisomerase VI},
  author={K. Corbett and P. Benedetti and J. Berger},
  journal={Nature Structural \&Molecular Biology},
  year={2007},
  volume={14},
  pages={611-619}
}
Type II topoisomerases help disentangle chromosomes to facilitate cell division. To advance understanding of the structure and dynamics of these essential enzymes, we have determined the crystal structure of an archaeal type IIB topoisomerase, topo VI, at 4.0-Å resolution. The 220-kDa heterotetramer adopts a 'twin-gate' architecture, in which a pair of ATPase domains at one end of the enzyme is poised to coordinate DNA movements into the enzyme and through a set of DNA-cleaving domains at the… Expand
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