Structural and functional characterization of Salmonella enterica serovar Typhimurium YcbL: An unusual Type II glyoxalase |
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| Authors: | Anna L Stamp Paul Owen Kamel El Omari Charles E Nichols Michael Lockyer Heather K Lamb Ian G Charles Alastair R Hawkins David K Stammers |
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| Affiliation: | 1Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, United Kingdom;2Institute of Cell and Molecular Biosciences, Catherine Cookson Building, Medical School, Framlington Place, Newcastle University, Newcastle-upon-Tyne NE2 4HH, United Kingdom;3Arrow Therapeutics, Britannia House, Trinity Street, Borough, London SE1 1DA, United Kingdom |
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| Abstract: | 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. |
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| Keywords: | YcbL glyoxalase II zinc metallohydrolase β‐lactamase Salmonella typhimurium crystal |
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