期刊
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
卷 72, 期 -, 页码 488-496出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2059798316001212
关键词
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
资金
- PTC Therapeutics Inc.
- Wellcome Trust Seeding Drug Discovery award [097753]
- Biotechnology and Biological Research Council [BB/H00405X/1, BB/K10069/1]
- BBSRC
- Biotechnology and Biological Sciences Research Council [BB/H00405X/1, BB/K010069/1] Funding Source: researchfish
- BBSRC [BB/H00405X/1, BB/K010069/1] Funding Source: UKRI
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 angstrom 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.
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