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2XKK

CRYSTAL STRUCTURE OF MOXIFLOXACIN, DNA, and A. BAUMANNII TOPO IV (PARE-PARC FUSION TRUNCATE)

Summary for 2XKK
Entry DOI10.2210/pdb2xkk/pdb
Related2XKJ
DescriptorTOPOISOMERASE IV, DNA, MAGNESIUM ION, ... (6 entities in total)
Functional Keywordsisomerase-dna-antibiotic complex, type iia topoisomerase, quinolone, antibacterial agent, isomerase/dna/antibiotic
Biological sourceACINETOBACTER BAUMANNII
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Total number of polymer chains4
Total formula weight194147.10
Authors
Wohlkonig, A.,Chan, P.F.,Fosberry, A.P.,Homes, P.,Huang, J.,Kranz, M.,Leydon, V.R.,Miles, T.J.,Pearson, N.D.,Perera, R.L.,Shillings, A.J.,Gwynn, M.N.,Bax, B.D. (deposition date: 2010-07-08, release date: 2010-09-01, Last modification date: 2024-11-06)
Primary citationWohlkonig, A.,Chan, P.F.,Fosberry, A.P.,Homes, P.,Huang, J.,Kranz, M.,Leydon, V.R.,Miles, T.J.,Pearson, N.D.,Perera, R.L.,Shillings, A.J.,Gwynn, M.N.,Bax, B.D.
Structural Basis of Quinolone Inhibition of Type Iia Topoisomerases and Target-Mediated Resistance
Nat.Struct.Mol.Biol., 17:1152-, 2010
Cited by
PubMed Abstract: Quinolone antibacterials have been used to treat bacterial infections for over 40 years. A crystal structure of moxifloxacin in complex with Acinetobacter baumannii topoisomerase IV now shows the wedge-shaped quinolone stacking between base pairs at the DNA cleavage site and binding conserved residues in the DNA cleavage domain through chelation of a noncatalytic magnesium ion. This provides a molecular basis for the quinolone inhibition mechanism, resistance mutations and invariant quinolone antibacterial structural features.
PubMed: 20802486
DOI: 10.1038/NSMB.1892
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.25 Å)
Structure validation

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