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1. Structural and functional characterization of Salmonella enterica serovar Typhimurium YcbL: An unusual Type II glyoxalase

Author

Stamp, AL, Owen, P, El Omari, K, Nichols, CE, Lockyer, M, Lamb, HK, Charles, IG, Hawkins, AR, and Stammers, DK

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

Published
2010

3. Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351.

Author

Stamp AL, Owen P, El Omari K, Lockyer M, Lamb HK, Charles IG, Hawkins AR, and Stammers DK

Subjects
Amino Acid Sequence, Arginine metabolism, Calorimetry, Crystallography, X-Ray, Molecular Sequence Data, Periplasmic Binding Proteins metabolism, Protein Binding, Salmonella typhi metabolism, Sequence Alignment, Arginine chemistry, Periplasmic Binding Proteins chemistry, Salmonella typhi chemistry
Published
2011
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4. Structural and functional characterization of Salmonella enterica serovar Typhimurium YcbL: an unusual Type II glyoxalase.

Author

Stamp AL, Owen P, El Omari K, Nichols CE, Lockyer M, Lamb HK, Charles IG, Hawkins AR, and Stammers DK

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

Published
2010
Full Text
View/download PDF

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