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Brief Communication
Nature Structural & Molecular Biology 16, 667–669 (1 June 2009) | doi:10.1038/nsmb.1604
Structural insight into the quinolone|[ndash]|DNA cleavage complex of type IIA topoisomerases
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Abstract
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.
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