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3RAE

Quinolone(Levofloxacin)-DNA cleavage complex of type IV topoisomerase from S. pneumoniae

Summary for 3RAE
Entry DOI10.2210/pdb3rae/pdb
Related2NOV 3FOE 3FOF 3K9F 3KSA 3KSB 3LTN 3RAD 3RAF
DescriptorDNA topoisomerase 4 subunit A, DNA topoisomerase 4 subunit B, 5'-D(*CP*AP*TP*GP*AP*AP*T)-3', ... (9 entities in total)
Functional Keywordsprotein-dna cleavage complex, topoisomerase iia, levofloxacin, isomerase-dna-antibiotic complex, isomerase/dna/antibiotic
Biological sourceStreptococcus pneumoniae
More
Cellular locationCell membrane ; Peripheral membrane protein : P72525
Total number of polymer chains8
Total formula weight185552.11
Authors
Laponogov, I.,Pan, X.-S.,Veselkov, D.A.,McAuley, K.E.,Fisher, L.M.,Sanderson, M.R. (deposition date: 2011-03-28, release date: 2012-04-25, Last modification date: 2024-10-30)
Primary citationVeselkov, D.A.,Laponogov, I.,Pan, X.S.,Selvarajah, J.,Skamrova, G.B.,Branstrom, A.,Narasimhan, J.,Prasad, J.V.,Fisher, L.M.,Sanderson, M.R.
Structure of a quinolone-stabilized cleavage complex of topoisomerase IV from Klebsiella pneumoniae and comparison with a related Streptococcus pneumoniae complex.
Acta Crystallogr.,Sect.D, 72:488-496, 2016
Cited by
PubMed 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.
PubMed: 27050128
DOI: 10.1107/S2059798316001212
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

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