Structure of the topoisomerase IV C-terminal domain: a broken beta-propeller implies a role as geometry facilitator in catalysis.

@article{Hsieh2004StructureOT,
  title={Structure of the topoisomerase IV C-terminal domain: a broken beta-propeller implies a role as geometry facilitator in catalysis.},
  author={T Hsieh and Lynn Farh and Wai Mun Huang and Nei-Li Chan},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 53},
  pages={55587-93}
}
Bacteria possess two closely related yet functionally distinct essential type IIA topoisomerases (Topos). DNA gyrase supports replication and transcription with its unique supercoiling activity, whereas Topo IV preferentially relaxes (+) supercoils and is a decatenating enzyme required for chromosome segregation. Here we report the crystal structure of the C-terminal domain of Topo IV ParC subunit (ParC-CTD) from Bacillus stearothermophilus and provide a structure-based explanation for how Topo… CONTINUE READING

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