3HBR
Crystal structure of OXA-48 beta-lactamase
Summary for 3HBR
| Entry DOI | 10.2210/pdb3hbr/pdb |
| Descriptor | OXA-48, 1,2-ETHANEDIOL (3 entities in total) |
| Functional Keywords | class d beta-lactamase, oxa-48, antibiotic, dimer, hydrolase |
| Biological source | Klebsiella pneumoniae |
| Total number of polymer chains | 4 |
| Total formula weight | 122007.17 |
| Authors | Calderone, V.,Mangani, S.,Benvenuti, M.,Rossolini, G.M.,Docquier, J.D. (deposition date: 2009-05-05, release date: 2009-06-23, Last modification date: 2023-11-22) |
| Primary citation | Docquier, J.D.,Calderone, V.,De Luca, F.,Benvenuti, M.,Giuliani, F.,Bellucci, L.,Tafi, A.,Nordmann, P.,Botta, M.,Rossolini, G.M.,Mangani, S. Crystal structure of the OXA-48 beta-lactamase reveals mechanistic diversity among class D carbapenemases. Chem.Biol., 16:540-547, 2009 Cited by PubMed Abstract: Carbapenem-hydrolyzing class D beta-lactamases (CHDLs) are enzymes found in important Gram-negative pathogens (mainly Acinetobacter baumannii and Enterobacteriaceae) that confer resistance to beta-lactam antibiotics, and notably carbapenems. The crystal structure of the OXA-48 carbapenemase was determined at pH 7.5 and at a resolution of 1.9 A. Surprisingly, and by contrast with OXA-24, the only other CHDL of known crystal structure, the structure of OXA-48 was similar to OXA-10, an enzyme devoid of carbapenemase activity, indicating that the hydrolysis of these compounds could depend on subtle changes in the active site region. Moreover, the active site groove of OXA-48 was different from that of OXA-24 in shape, dimensions, and charge distribution. Molecular dynamics pointed to the functional relevance of residues located in or close to the beta5-beta6 loop and allowed us to propose a mechanism for carbapenem hydrolysis by OXA-48. PubMed: 19477418DOI: 10.1016/j.chembiol.2009.04.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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