We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Structural insight into the quinolone–DNA cleavage complex of type IIA topoisomerases.
- Authors
Laponogov, Ivan; Sohi, Maninder K; Veselkov, Dennis A.; Pan, Xiao-Su; Sawhney, Ritica; Thompson, Andrew W.; McAuley, Katherine E.; Fisher, L. Mark; Sanderson, Mark R.
- 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. These structures reveal two drug molecules intercalated at the highly bent DNA gate and help explain antibacterial quinolone action and resistance.
- Subjects
DNA topoisomerase II; QUINOLONE antibacterial agents; TRANSCRIPTION factors; BACTERIAL chromosomes; ISOMERASES
- Publication
Nature Structural & Molecular Biology, 2009, Vol 16, Issue 6, p667
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb.1604