Structure of a quinolone-stabilized cleavage complex of topoisomerase IV from Klebsiella pneumoniae and comparison with a related Streptococcus pneumoniae complex.
Author(s)
Type
Journal Article
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.
Date Issued
2016-04-01
Date Acceptance
2016-01-19
Citation
Acta Crystallographica Section D, 2016, 72 (Pt 4), pp.488-496
ISSN
2059-7983
Publisher
International Union of Crystallography
Start Page
488
End Page
496
Journal / Book Title
Acta Crystallographica Section D
Volume
72
Issue
Pt 4
Copyright Statement
This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.
License URL
Identifier
PII: S2059798316001212
Subjects
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
Publication Status
Published