Structural insight into the quinolone–DNA cleavage complex of type IIA topoisomerases

@article{Laponogov2009StructuralII,
  title={Structural insight into the quinolone–DNA cleavage complex of type IIA topoisomerases},
  author={Ivan Laponogov and Maninder K. Sohi and Dennis A. Veselkov and X S Pan and Ritica Sawhney and Andrew W Thompson and Katherine E McAuley and L Mark Fisher and Mark R Sanderson},
  journal={Nature Structural \&Molecular Biology},
  year={2009},
  volume={16},
  pages={667-669}
}
Type II topoisomerases alter DNA topology by forming a covalent DNA-cleavage complex that allows DNA transport through a double-stranded DNA break. We present the structures of cleavage complexes formed by the Streptococcus pneumoniae ParC breakage-reunion and ParE TOPRIM domains of topoisomerase IV stabilized by moxifloxacin and clinafloxacin, two antipneumococcal fluoroquinolones. These structures reveal two drug molecules intercalated at the highly bent DNA gate and help explain… Expand
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TLDR
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TLDR
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TLDR
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TLDR
Recent advances in mechanistic insights into topoisomerases are covered, including a DNA helicase capable of modulating the directionality of strand passage, enabling important functions like reannealing denatured DNA and resolving recombination intermediates. Expand
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