title: Metallo-beta-lactamase: structure and mechanism.
abstract: This past year has produced determinations of X-ray crystal structures for three metallo-beta-lactamases and the elucidation of the catalytic mechanisms for a monozinc and a dizinc enzyme. These advances shed light on how such a diverse group of enzymes are evolving to inactivate so efficiently a broad spectrum of beta-lactam antibiotics.
authors.affiliation: The Pennsylvania State University, Department of Chemistry, 152 Davey Laboratory, University Park, PA 16802, USA.
authors.forename: Z
authors.initials: Z
authors.lastname: Wang
authors.forename: W
authors.initials: W
authors.lastname: Fast
authors.forename: A M
authors.initials: AM
authors.lastname: Valentine
authors.forename: S J
authors.initials: SJ
authors.lastname: Benkovic
mesh_terms: D000595:Amino Acid Sequence; D002384:Catalysis; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment; D013329:Structure-Activity Relationship; D001618:beta-Lactamases / Q000737:chemistry / Q000378:metabolism*
chemical_list: D001618:beta-Lactamases