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YcbL has been annotated as either a metallo-β-lactamase or glyoxalase II (GLX2), both members of the zinc metallohydrolase superfamily, that contains many enzymes with a diverse range of activities. Here, we report crystallographic and biochemical data for Salmonella enterica serovar Typhimurium YcbL that establishes it as GLX2, which differs in certain structural and functional properties compared with previously known examples. These features include the insertion of an α-helix after residue 87 in YcbL and truncation of the C-terminal domain, which leads to the loss of some recognition determinants for the glutathione substrate. Despite these changes, YcbL has robust GLX2 activity. A further difference is that the YcbL structure contains only a single bound metal ion rather than the dual site normally observed for GLX2s. Activity assays in the presence of various metal ions indicate an increase in activity above basal levels in the presence of manganous and ferrous ions. Thus, YcbL represents a novel member of the GLX2 family.

Original publication

DOI

10.1002/pro.475

Type

Journal article

Journal

Protein Sci

Publication Date

10/2010

Volume

19

Pages

1897 - 1905

Keywords

Amino Acid Sequence, Bacterial Proteins, Binding Sites, Crystallography, X-Ray, Enzyme Assays, Kinetics, Metals, Models, Molecular, Molecular Sequence Data, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Salmonella typhimurium, Sequence Homology, Amino Acid, Substrate Specificity, Thiolester Hydrolases, Zinc