6fm7
Crystal structure of the class C beta-lactamase TRU-1 from Aeromonas enteropelogenes in complex with avibactamCrystal structure of the class C beta-lactamase TRU-1 from Aeromonas enteropelogenes in complex with avibactam
Structural highlights
Publication Abstract from PubMedbeta-lactamases (BLs) are important antibiotic resistance determinants that significantly compromise the efficacy of valuable beta-lactam antibacterial drugs. For that reason, combinations with beta-lactamase inhibitor were developed. Avibactam is the first non-beta-lactam BL inhibitor introduced in clinical practice. Ceftazidime-avibactam represents one of the few last-resort antibiotics available for the treatment of infections caused by near pandrug-resistant bacteria. TRU-1 is a chromosomally-encoded AmpC-type BL of Aeromonas enteropelogenes, related to the FOX-type BLs and constitutes a good model for class C BLs. TRU-1 crystals provided ultra-high resolution diffraction data for the native enzyme and for its complex with avibactam. The comparison of the native and avibactam-bound structures revealed new details in the conformations of residues relevant for substrate and/or inhibitor binding. Furthermore, the comparison of the TRU-1 and P. aeruginosa AmpC avibactam-bound structures revealed two inhibitor conformations likely corresponding to two different states occurring during inhibitor carbamylation/recyclization. The Atomic Resolution Structure of a Class C beta-lactamase and of its Complex with Avibactam.,Mangani S, Pozzi C, Di Pisa F, De Luca F, Benvenuti M, Docquier JD ChemMedChem. 2018 May 22. doi: 10.1002/cmdc.201800213. PMID:29786960[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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