3RAE
Quinolone(Levofloxacin)-DNA cleavage complex of type IV topoisomerase from S. pneumoniae
Summary for 3RAE
Entry DOI | 10.2210/pdb3rae/pdb |
Related | 2NOV 3FOE 3FOF 3K9F 3KSA 3KSB 3LTN 3RAD 3RAF |
Descriptor | DNA topoisomerase 4 subunit A, DNA topoisomerase 4 subunit B, 5'-D(*CP*AP*TP*GP*AP*AP*T)-3', ... (9 entities in total) |
Functional Keywords | protein-dna cleavage complex, topoisomerase iia, levofloxacin, isomerase-dna-antibiotic complex, isomerase/dna/antibiotic |
Biological source | Streptococcus pneumoniae More |
Cellular location | Cell membrane ; Peripheral membrane protein : P72525 |
Total number of polymer chains | 8 |
Total formula weight | 185552.11 |
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 citation | Veselkov, 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: 27050128DOI: 10.1107/S2059798316001212 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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