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Structure of a quinolone-stabilized cleavage complex of topoisomerase IV from Klebsiella pneumoniae and comparison with a related Streptococcus pneumoniae complex.

Veselkov, DA; Laponogov, I; Pan, XS; Selvarajah, J; Skamrova, GB; Branstrom, A; Narasimhan, J; Prasad, JV; Fisher, LM; Sanderson, MR (2016) Structure of a quinolone-stabilized cleavage complex of topoisomerase IV from Klebsiella pneumoniae and comparison with a related Streptococcus pneumoniae complex. Acta Crystallographica Section D Structural Biology, 72 (Pt 4). pp. 488-496. ISSN 2059-7983 https://doi.org/10.1107/S2059798316001212
SGUL Authors: Fisher, Larry Mark Pan, Xiao Su Selvarajah, Jogitha

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Abstract

Klebsiella pneumoniae is a Gram-negative bacterium that is responsible for a range of common infections, including pulmonary pneumonia, bloodstream infections and meningitis. Certain strains of Klebsiella have become highly resistant to antibiotics. Despite the vast amount of research carried out on this class of bacteria, the molecular structure of its topoisomerase IV, a type II topoisomerase essential for catalysing chromosomal segregation, had remained unknown. In this paper, the structure of its DNA-cleavage complex is reported at 3.35 Å resolution. The complex is comprised of ParC breakage-reunion and ParE TOPRIM domains of K. pneumoniae topoisomerase IV with DNA stabilized by levofloxacin, a broad-spectrum fluoroquinolone antimicrobial agent. This complex is compared with a similar complex from Streptococcus pneumoniae, which has recently been solved.

Item Type: Article
Additional Information: Open access article under an open-access licence identical to the Creative Commons Attribution Licence http://creativecommons.org/licenses/by/2.0/uk/legalcode This Creative Commons England and Wales Public Licence enables you to view, edit, modify, translate and distribute Works worldwide, provided that you credit the Original Author
Keywords: DNA binding, Gram-negative complexes, Klebsiella pneumoniae, X-ray crystallography, cleavage complex, isomerase, isomerase–DNA complex, levofloxacin, protein–DNA–drug complexes, quinolone, topoisomerase IV, topoisomerases
SGUL Research Institute / Research Centre: Academic Structure > Molecular and Clinical Sciences Research Institute (MCS)
Academic Structure > Molecular and Clinical Sciences Research Institute (MCS) > Cell Sciences (INCCCS)
Journal or Publication Title: Acta Crystallographica Section D Structural Biology
ISSN: 2059-7983
Language: eng
Dates:
DateEvent
1 April 2016Published
Publisher License: Publisher's own licence
Projects:
Project IDFunderFunder ID
097753Wellcome Trusthttp://dx.doi.org/10.13039/100004440
BB/H00405X/1Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/K10069/1Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
PubMed ID: 27050128
Go to PubMed abstract
URI: https://openaccess.sgul.ac.uk/id/eprint/107853
Publisher's version: https://doi.org/10.1107/S2059798316001212

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