9RAO
Class A CTX-M-14 E166A mutant in complex with Cloxacillin at room temperature
Summary for 9RAO
| Entry DOI | 10.2210/pdb9rao/pdb |
| Descriptor | Beta-lactamase, CLOXACILLIN (OPEN FORM) (3 entities in total) |
| Functional Keywords | antibiotic resistance, class a beta-lactamase, isoxazolyl penicillins, protein binding |
| Biological source | Klebsiella pneumoniae |
| Total number of polymer chains | 1 |
| Total formula weight | 31389.15 |
| Authors | |
| Primary citation | Gore, G.,Prester, A.,von Stetten, D.,Bartels, K.,Schulz, E.C. Binding mode of Isoxazolyl Penicillins to a Class-A beta-lactamase at ambient conditions. Commun Chem, 8:387-387, 2025 Cited by PubMed Abstract: The predominant resistance mechanism observed in Gram-negative bacteria involves the production of β-lactamases, which catalyse the hydrolysis of β-lactam antibiotics, thereby rendering them ineffective. Although Isoxazolyl Penicillins have been available since the 1970s, there are currently no structures in complex with class-A β-lactamases available. Here we have analysed the structure of the clinically relevant β-lactamase CTX-M-14 from Klebsiella pneumoniae near physiological temperatures, via serial synchrotron crystallography. We demonstrate the acyl-enzyme intermediates of the catalytically impaired CTX-M-14 mutant E166A in complex with three Isoxazolyl-Penicillins: Oxacillin, Cloxacillin and Dicloxacillin. Structural comparisons of CTX-M-Penicillin complexes show that, while conserved active-site interactions are maintained, each Isoxazolyl-Penicillin adopts a distinct conformation. While the three derivatives differ only by one and two chlorine atoms, respectively, their conformational heterogeneity appears to be increased by chlorination of the phenyl ring. PubMed: 41326695DOI: 10.1038/s42004-025-01801-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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