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3FOE

Structural insight into the quinolone-DNA cleavage complex of type IIA topoisomerases

Summary for 3FOE
Entry DOI10.2210/pdb3foe/pdb
Related2NOV 3FOF
DescriptorDNA topoisomerase 4 subunit A, DNA topoisomerase 4 subunit B, DNA (5'-D(P*AP*CP*CP*AP*AP*GP*GP*TP*CP*AP*TP*GP*AP*AP*T)-3'), ... (7 entities in total)
Functional Keywordsquinolone, topoisomerase, dna, protein-dna cleavage complex, streptococcus pneumoniae, clinafloxacin, cell membrane, dna-binding, isomerase, membrane, atp-binding, nucleotide-binding, isomerase-dna complex, isomerase/dna
Biological sourceStreptococcus pneumoniae
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Cellular locationCell membrane; Peripheral membrane protein (By similarity): P72525
Total number of polymer chains8
Total formula weight195299.44
Authors
Laponogov, I.,Sohi, M.K.,Veselkov, D.A.,Pan, X.-S.,Sawhney, R.,Thompson, A.W.,McAuley, K.E.,Fisher, L.M.,Sanderson, M.R. (deposition date: 2008-12-30, release date: 2009-02-24, Last modification date: 2023-11-01)
Primary citationLaponogov, I.,Sohi, M.K.,Veselkov, D.A.,Pan, X.-S.,Sawhney, R.,Thompson, A.W.,McAuley, K.E.,Fisher, L.M.,Sanderson, M.R.
Structural insight into the quinolone-DNA cleavage complex of type IIA topoisomerases
Nat.Struct.Mol.Biol., 16:667-669, 2009
Cited by
PubMed Abstract: Type II topoisomerases alter DNA topology by forming a covalent DNA-cleavage complex that allows DNA transport through a double-stranded DNA break. We present the structures of cleavage complexes formed by the Streptococcus pneumoniae ParC breakage-reunion and ParE TOPRIM domains of topoisomerase IV stabilized by moxifloxacin and clinafloxacin, two antipneumococcal fluoroquinolones. These structures reveal two drug molecules intercalated at the highly bent DNA gate and help explain antibacterial quinolone action and resistance.
PubMed: 19448616
DOI: 10.1038/nsmb.1604
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4.001 Å)
Structure validation

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