5FQB
Crystal Structure of Bacillus cereus Metallo-Beta-Lactamase with 2C
Summary for 5FQB
| Entry DOI | 10.2210/pdb5fqb/pdb |
| Related | 5FQA |
| Descriptor | BETA-LACTAMASE 2, ZINC ION, (4~{R})-4-[[4-(aminomethyl)phenyl]carbonylamino]-3,3-bis(oxidanyl)-2-oxa-3-boranuidabicyclo[4.4.0]deca-1(10),6,8-triene-10-carboxylic acid, ... (6 entities in total) |
| Functional Keywords | hydrolase, antibiotic resistance, lactamase |
| Biological source | BACILLUS CEREUS |
| Total number of polymer chains | 1 |
| Total formula weight | 25671.65 |
| Authors | Cahill, S.T.,Brem, J.,McDonough, M.A.,Schofield, C.J. (deposition date: 2015-12-08, release date: 2016-08-10, Last modification date: 2024-01-10) |
| Primary citation | Brem, J.,Cain, R.,Cahill, S.,McDonough, M.A.,Clifton, I.J.,Jimenez-Castellanos, J.C.,Avison, M.B.,Spencer, J.,Fishwick, C.W.,Schofield, C.J. Structural basis of metallo-beta-lactamase, serine-beta-lactamase and penicillin-binding protein inhibition by cyclic boronates. Nat Commun, 7:12406-12406, 2016 Cited by PubMed Abstract: β-Lactamases enable resistance to almost all β-lactam antibiotics. Pioneering work revealed that acyclic boronic acids can act as 'transition state analogue' inhibitors of nucleophilic serine enzymes, including serine-β-lactamases. Here we report biochemical and biophysical analyses revealing that cyclic boronates potently inhibit both nucleophilic serine and zinc-dependent β-lactamases by a mechanism involving mimicking of the common tetrahedral intermediate. Cyclic boronates also potently inhibit the non-essential penicillin-binding protein PBP 5 by the same mechanism of action. The results open the way for development of dual action inhibitors effective against both serine- and metallo-β-lactamases, and which could also have antimicrobial activity through inhibition of PBPs. PubMed: 27499424DOI: 10.1038/ncomms12406 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.899 Å) |
Structure validation
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