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 it 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 3.35Å resolution. The complex is comprised of ParC breakage-reunion and ParE TOPRIM domains of it K. pneumoniae topoisomerase IV with DNA stabilized by levofloxacin, a broad-spectrum fluoroquinolone antimicrobial agent. This complex is compared with a similar complex from it Streptococcus pneumoniae, which has recently been solved.
Original language | English |
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Pages (from-to) | 488-496 |
Number of pages | 9 |
Journal | Acta Crystallographica Section D Structural Biology |
Volume | 72 |
Issue number | 4 |
Early online date | 24 Mar 2016 |
DOIs | |
Publication status | Published - 2016 |
Keywords
- Klebsiella pneumoniae, cleavage complex, quinolone, levofloxacin, topoisomerase IV, DNA binding, isomerase, isomerase-DNA complex, topoisomerases, Gram-negative complexes, X-ray crystallography, protein-DNA-drug complexes