Acta Crystallogr D Struct Biol. 2016 Apr 1;72(Pt 4):488-96. doi: 10.1107/S2059798316001212. Epub 2016 Mar 24.

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

Veselkov DA1, Laponogov I1, Pan XS2, Selvarajah J2, Skamrova GB1, Branstrom A3, Narasimhan J3, Prasad JV3, Fisher LM2, Sanderson MR1.

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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.

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

PMID: 27050128 [PubMed - in process]