7b3s | pdb_00007b3s

OXA-10 beta-lactamase with S67Dha modification

spinqualitylabelsall models 7b3s, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7b3s is a 2 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: CO2, DHA, KCX, NA, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BLO10_PSEAI Hydrolyzes both carbenicillin and oxacillin. Publication Abstract from PubMed SignificanceMicrobial resistance to beta-lactam antibiotics mediated by beta-lactamase-catalyzed hydrolysis is a major global health concern. Penam sulfones, which are structurally related to penicillins, inhibit clinically important serine beta-lactamases (SBLs) by forming transiently stable covalent complexes, thereby protecting beta-lactam antibiotics from hydrolysis. The characterization of these complexes and mechanisms of SBL inhibition is important for development of new SBL inhibitors (SBLi). Studies on the mechanism of the new SBLi enmetazobactam employing mass spectrometry and X-ray crystallography inform on its mode of action and also lead to reevaluation of mechanisms of current clinically important SBLi. In addition to insights into the mechanisms of transient SBL inhibition by penam sulfones, the results reveal potential for penam sulfone optimization to enable irreversible SBL inhibition. Studies on enmetazobactam clarify mechanisms of widely used beta-lactamase inhibitors.,Lang PA, Raj R, Tumber A, Lohans CT, Rabe P, Robinson CV, Brem J, Schofield CJ Proc Natl Acad Sci U S A. 2022 May 3;119(18):e2117310119. doi:, 10.1073/pnas.2117310119. Epub 2022 Apr 29. PMID:35486701 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-lactamase 3D structures

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