2XKJ
CRYSTAL STRUCTURE OF CATALYTIC CORE OF A. BAUMANNII TOPO IV (PARE- PARC FUSION TRUNCATE)
Summary for 2XKJ
Entry DOI | 10.2210/pdb2xkj/pdb |
Related | 2XKK |
Descriptor | TOPOISOMERASE IV, SULFATE ION, GLYCEROL, ... (4 entities in total) |
Functional Keywords | isomerase, type iia topoisomerase |
Biological source | ACINETOBACTER BAUMANNII |
Total number of polymer chains | 1 |
Total formula weight | 86369.99 |
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 citation | 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. 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: 20802486DOI: 10.1038/NSMB.1892 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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