Holoenzyme assembly and ATP-mediated conformational dynamics of topoisomerase VI

@article{Corbett2007HoloenzymeAA,
  title={Holoenzyme assembly and ATP-mediated conformational dynamics of topoisomerase VI},
  author={Kevin D. Corbett and Pier Giuseppe De Benedetti and James M. 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… 
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SURVEY AND SUMMARY The ancestral role of ATP hydrolysis in type II topoisomerases: prevention of DNA double-strand breaks
TLDR
It is proposed that the energy of ATP hydrolysis is needed to control the separation of protein–protein interfaces and prevent the accidental formation of potentially mutagenic or cytotoxic DSBs.
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