title: Structure of New Delhi metallo-β-lactamase 1 (NDM-1).
abstract: Antibiotic resistance in bacterial pathogens poses a serious threat to human health and the metallo-β-lactamase (MBL) enzymes are responsible for much of this resistance. The recently identified New Delhi MBL 1 (NDM-1) is a novel member of this family that is capable of hydrolysing a wide variety of clinically important antibiotics. Here, the crystal structure of NDM-1 from Klebsiella pneumoniae is reported and its structure and active site are discussed in the context of other recently deposited coordinates of NDM-1.
authors.affiliation: Research Complex at Harwell, Rutherford Appleton Laboratory, Harwell Oxford, Didcot, Oxon OX11 0FA, England.
authors.forename: Victoria L
authors.initials: VL
authors.lastname: Green
authors.forename: Anil
authors.initials: A
authors.lastname: Verma
authors.forename: Raymond J
authors.initials: RJ
authors.lastname: Owens
authors.forename: Simon E V
authors.initials: SE
authors.lastname: Phillips
authors.forename: Stephen B
authors.initials: SB
authors.lastname: Carr
mesh_terms: D055162:Biocatalysis; D018360:Crystallography, X-Ray; D007711:Klebsiella pneumoniae / Q000201:enzymology*; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D001618:beta-Lactamases / Q000737:chemistry*
chemical_list: D001618:beta-Lactamases; C552864:beta-lactamase NDM-1
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