Brief Communication abstract
Nature Structural & Molecular Biology 16, 667 - 669 (2009)
Published online: 17 May 2009 | doi:10.1038/nsmb.1604
Structural insight into the quinolone–DNA cleavage complex of type IIA topoisomerases
Ivan Laponogov1,2, Maninder K Sohi1, Dennis A Veselkov1, Xiao-Su Pan2, Ritica Sawhney2, Andrew W Thompson3, Katherine E McAuley4, L Mark Fisher2 & Mark R Sanderson1
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 antibacterial quinolone action and resistance.
- Randall Division of Cell and Molecular Biophysics, King's College London, University of London, London, UK.
- Molecular Genetics Group, Molecular and Metabolic Signalling Centre, Division of Basic Medical Sciences, St. George's, University of London, London, UK.
- Synchrotron SOLEIL, L'Orme de Merisiers, Saint Aubin-BP48, Gif-sur-Yvette CEDEX, France.
- Beamline I03, Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Oxfordshire, UK.
Correspondence to: L Mark Fisher2 e-mail: lfisher@sgul.ac.uk
Correspondence to: Mark R Sanderson1 e-mail: mark.sanderson@kcl.ac.uk
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