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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2009-06

AUTHORS

Ivan Laponogov, Maninder K Sohi, Dennis A Veselkov, Xiao-Su Pan, Ritica Sawhney, Andrew W Thompson, Katherine E McAuley, L Mark Fisher, Mark R Sanderson

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. More... »

PAGES

667-669

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb.1604

DOI

http://dx.doi.org/10.1038/nsmb.1604

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1029322394

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/19448616


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