title: Complete ¹H, ¹⁵N, and ¹³C resonance assignments of Bacillus cereus metallo-β-lactamase and its complex with the inhibitor R-thiomandelic acid.
abstract: β-Lactamases inactivate β-lactam antibiotics by hydrolysis of their endocyclic β-lactam bond and are a major cause of antibiotic resistance in pathogenic bacteria. The zinc dependent metallo-β-lactamase enzymes are of particular concern since they are located on highly transmissible plasmids and have a broad spectrum of activity against almost all β-lactam antibiotics. We present here essentially complete (>96%) backbone and sidechain sequence-specific NMR resonance assignments for the Bacillus cereus subclass B1 metallo-β-lactamase, BcII, and for its complex with R-thiomandelic acid, a broad spectrum inhibitor of metallo-β-lactamases. These assignments have been used as the basis for determination of the solution structures of the enzyme and its inhibitor complex and can also be used in a rapid screen for other metallo-β-lactamase inhibitors.
authors.affiliation: The Henry Wellcome Laboratories of Structural Biology, Department of Biochemistry, University of Leicester, Lancaster Road, PO Box 138, Leicester, LE1 9HN, UK.
authors.forename: Andreas Ioannis
authors.initials: AI
authors.lastname: Karsisiotis
authors.forename: Christian
authors.initials: C
authors.lastname: Damblon
authors.forename: Gordon C K
authors.initials: GC
authors.lastname: Roberts
mesh_terms: D001409:Bacillus cereus / Q000201:enzymology*; D008333:Mandelic Acids / Q000378:metabolism* / Q000494:pharmacology*; D019906:Nuclear Magnetic Resonance, Biomolecular; D013438:Sulfhydryl Compounds / Q000378:metabolism* / Q000494:pharmacology*; D065093:beta-Lactamase Inhibitors / Q000378:metabolism / Q000494:pharmacology; D001618:beta-Lactamases / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D008333:Mandelic Acids; D013438:Sulfhydryl Compounds; D065093:beta-Lactamase Inhibitors; C443128:thiomandelic acid; D001618:beta-Lactamases