7KER
avibactam-CDD-1 45 minute complex
Summary for 7KER
| Entry DOI | 10.2210/pdb7ker/pdb |
| Descriptor | Beta-lactamase, (2S,5R)-1-formyl-5-[(sulfooxy)amino]piperidine-2-carboxamide, (2S,5R)-7-oxo-6-(sulfooxy)-1,6-diazabicyclo[3.2.1]octane-2-carboxamide, ... (7 entities in total) |
| Functional Keywords | antibiotic resistance, mutant, gram-positive, inhibitor, hydrolase, hydrolase-inhibitor complex, hydrolase/inhibitor |
| Biological source | Clostridioides difficile |
| Total number of polymer chains | 1 |
| Total formula weight | 37412.35 |
| Authors | Smith, C.A.,Vakulenko, S.B.,Stewart, N.K.,Toth, M. (deposition date: 2020-10-12, release date: 2021-01-20, Last modification date: 2025-04-02) |
| Primary citation | Stewart, N.K.,Toth, M.,Stasyuk, A.,Lee, M.,Smith, C.A.,Vakulenko, S.B. Inhibition of the Clostridioides difficile Class D beta-Lactamase CDD-1 by Avibactam. Acs Infect Dis., 7:1164-1176, 2021 Cited by PubMed Abstract: Avibactam is a potent diazobicyclooctane inhibitor of class A and C β-lactamases. The inhibitor also exhibits variable activity against some class D enzymes from Gram-negative bacteria; however, its interaction with recently discovered class D β-lactamases from Gram-positive bacteria has not been studied. Here, we describe microbiological, kinetic, and mass spectrometry studies of the interaction of avibactam with CDD-1, a class D β-lactamase from the clinically important pathogen , and show that avibactam is a potent irreversible mechanism-based inhibitor of the enzyme. X-ray crystallographic studies at three time-points demonstrate the rapid formation of a stable CDD-1-avibactam acyl-enzyme complex and highlight differences in the anchoring of the inhibitor by class D enzymes from Gram-positive and Gram-negative bacteria. PubMed: 33390002DOI: 10.1021/acsinfecdis.0c00714 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.93 Å) |
Structure validation
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