Structural highlights
7ker is a 1 chain structure with sequence from "bacillus_difficilis"_hall_and_o'toole_1935 "bacillus difficilis" hall and o'toole 1935. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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Ligands: | , , , , |
NonStd Res: | |
Gene: | blaR1_4, blaR1_1, E5F39_11445, SAMEA2239407_03320, SAMEA3374989_01677 ("Bacillus difficilis" Hall and O'Toole 1935) |
Activity: | Beta-lactamase, with EC number 3.5.2.6 |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Publication Abstract from PubMed
Avibactam is a potent diazobicyclooctane inhibitor of class A and C beta-lactamases. The inhibitor also exhibits variable activity against some class D enzymes from Gram-negative bacteria; however, its interaction with recently discovered class D beta-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 beta-lactamase from the clinically important pathogen Clostridioides difficile, 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.
Inhibition of the Clostridioides difficile Class D beta-Lactamase CDD-1 by Avibactam.,Stewart NK, Toth M, Stasyuk A, Lee M, Smith CA, Vakulenko SB ACS Infect Dis. 2021 Jan 3. doi: 10.1021/acsinfecdis.0c00714. PMID:33390002[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stewart NK, Toth M, Stasyuk A, Lee M, Smith CA, Vakulenko SB. Inhibition of the Clostridioides difficile Class D beta-Lactamase CDD-1 by Avibactam. ACS Infect Dis. 2021 Jan 3. doi: 10.1021/acsinfecdis.0c00714. PMID:33390002 doi:http://dx.doi.org/10.1021/acsinfecdis.0c00714