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2XKJ

CRYSTAL STRUCTURE OF CATALYTIC CORE OF A. BAUMANNII TOPO IV (PARE- PARC FUSION TRUNCATE)

Summary for 2XKJ
Entry DOI10.2210/pdb2xkj/pdb
Related2XKK
DescriptorTOPOISOMERASE IV, SULFATE ION, GLYCEROL, ... (4 entities in total)
Functional Keywordsisomerase, type iia topoisomerase
Biological sourceACINETOBACTER BAUMANNII
Total number of polymer chains1
Total formula weight86369.99
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: 2023-12-20)
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 (2.2 Å)
Structure validation

227111

數據於2024-11-06公開中

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