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6FM7

Crystal structure of the class C beta-lactamase TRU-1 from Aeromonas enteropelogenes in complex with avibactam

Summary for 6FM7
Entry DOI10.2210/pdb6fm7/pdb
Related6FM6
DescriptorBeta-lactamase, (2S,5R)-1-formyl-5-[(sulfooxy)amino]piperidine-2-carboxamide, SULFATE ION, ... (5 entities in total)
Functional Keywordsavibactam, nxl, serine beta-lactamase, tru-1, class c, aeromonas enteropelogenes, hydrolase
Biological sourceAeromonas enteropelogenes (Aeromonas trota)
Total number of polymer chains1
Total formula weight42405.31
Authors
Pozzi, C.,De Luca, F.,Benvenuti, M.,Di Pisa, F.,Docquier, J.D.,Mangani, S. (deposition date: 2018-01-30, release date: 2018-05-30, Last modification date: 2024-11-13)
Primary citationPozzi, C.,Di Pisa, F.,De Luca, F.,Benvenuti, M.,Docquier, J.D.,Mangani, S.
Atomic-Resolution Structure of a Class C beta-Lactamase and Its Complex with Avibactam.
ChemMedChem, 13:1437-1446, 2018
Cited by
PubMed Abstract: β-Lactamases (BLs) are important antibiotic-resistance determinants that significantly compromise the efficacy of valuable β-lactam antibacterial drugs. Thus, combinations with BL inhibitor were developed. Avibactam is the first non-β-lactam BL inhibitor introduced into 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 ultrahigh-resolution diffraction data for the native enzyme and for its complex with avibactam. A comparison of the native and avibactam-bound structures revealed new details in the conformations of residues relevant for substrate and/or inhibitor binding. Furthermore, a comparison of the TRU-1 and Pseudomonas aeruginosa AmpC avibactam-bound structures revealed two inhibitor conformations that were likely to correspond to two different states occurring during inhibitor carbamylation/recyclization.
PubMed: 29786960
DOI: 10.1002/cmdc.201800213
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.04 Å)
Structure validation

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