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5EIX

QUINOLONE-STABILIZED CLEAVAGE COMPLEX OF TOPOISOMERASE IV FROM KLEBSIELLA PNEUMONIAE

Summary for 5EIX
Entry DOI10.2210/pdb5eix/pdb
Related3LTN 3RAD 3RAE 3RAF 4I3H
DescriptorDNA topoisomerase 4 subunit B,DNA topoisomerase 4 subunit A, SYMMETRISED E-SITE (PRE-CUT), MAGNESIUM ION, ... (5 entities in total)
Functional Keywordsklebsiella pneumoniae, cleavage complex, quinolone, levofloxacin, topoisomerase iv, dna binding, isomerase, isomerase-dna complex, isomerase/dna
Biological sourceKlebsiella pneumoniae
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Cellular locationCell membrane ; Peripheral membrane protein : R4YE07
Total number of polymer chains12
Total formula weight361652.64
Authors
Veselkov, D.A.,Laponogov, I.,Pan, X.-S.,Selvarajah, J.,Branstrom, A.,Fisher, L.M.,Sanderson, M.R. (deposition date: 2015-10-30, release date: 2016-04-13, Last modification date: 2024-05-08)
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 D Struct Biol, 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 (3.35 Å)
Structure validation

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