5fqb | pdb_00005fqb

Crystal Structure of Bacillus cereus Metallo-Beta-Lactamase with 2C

spinqualitylabelsall models 5fqb, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fqb is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, OK3, SO4, ZN Related: 5fqa Activity: Beta-lactamase, with EC number 3.5.2.6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BLA2_BACCE] Can hydrolyze carbapenem compounds. Publication Abstract from PubMed beta-Lactamases enable resistance to almost all beta-lactam antibiotics. Pioneering work revealed that acyclic boronic acids can act as 'transition state analogue' inhibitors of nucleophilic serine enzymes, including serine-beta-lactamases. Here we report biochemical and biophysical analyses revealing that cyclic boronates potently inhibit both nucleophilic serine and zinc-dependent beta-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-beta-lactamases, and which could also have antimicrobial activity through inhibition of PBPs. Structural basis of metallo-beta-lactamase, serine-beta-lactamase and penicillin-binding protein inhibition by cyclic boronates.,Brem J, Cain R, Cahill S, McDonough MA, Clifton IJ, Jimenez-Castellanos JC, Avison MB, Spencer J, Fishwick CW, Schofield CJ Nat Commun. 2016 Aug 8;7:12406. doi: 10.1038/ncomms12406. PMID:27499424 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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