1X8I
Crystal Structure of the Zinc Carbapenemase CphA in Complex with the Antibiotic Biapenem
Summary for 1X8I
| Entry DOI | 10.2210/pdb1x8i/pdb |
| Related | 1X8G 1X8H |
| Descriptor | Beta-lactamase, ZINC ION, SULFATE ION, ... (6 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Aeromonas hydrophila |
| Cellular location | Periplasm (Probable): P26918 |
| Total number of polymer chains | 1 |
| Total formula weight | 26268.07 |
| Authors | Garau, G.,Dideberg, O. (deposition date: 2004-08-18, release date: 2004-12-28, Last modification date: 2024-04-03) |
| Primary citation | Garau, G.,Bebrone, C.,Anne, C.,Galleni, M.,Frere, J.M.,Dideberg, O. A Metallo-beta-lactamase Enzyme in Action: Crystal Structures of the Monozinc Carbapenemase CphA and its Complex with Biapenem J.Mol.Biol., 345:785-795, 2005 Cited by PubMed Abstract: One strategy developed by bacteria to resist the action of beta-lactam antibiotics is the expression of metallo-beta-lactamases. CphA from Aeromonas hydrophila is a member of a clinically important subclass of metallo-beta-lactamases that have only one zinc ion in their active site and for which no structure is available. The crystal structures of wild-type CphA and its N220G mutant show the structural features of the active site of this enzyme, which is modeled specifically for carbapenem hydrolysis. The structure of CphA after reaction with a carbapenem substrate, biapenem, reveals that the enzyme traps a reaction intermediate in the active site. These three X-ray structures have allowed us to propose how the enzyme recognizes carbapenems and suggest a mechanistic pathway for hydrolysis of the beta-lactam. This will be relevant for the design of metallo-beta-lactamase inhibitors as well as of antibiotics that escape their hydrolytic activity. PubMed: 15588826DOI: 10.1016/j.jmb.2004.10.070 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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