Structural and functional characterization of Salmonella enterica serovar typhimurium YcbL: an unusual type II glyoxalase

Stamp, Anna L., Owen, Paul, El Omari, Kamel, Nichols, Charles E., Lockyer, Michael, Lamb, Heather K., Charles, Ian G., Hawkins, Alastair R. and Stammers, David K. (2010) Structural and functional characterization of Salmonella enterica serovar typhimurium YcbL: an unusual type II glyoxalase. Protein Science, 19 10: 1897-1905. doi:10.1002/pro.475


Author Stamp, Anna L.
Owen, Paul
El Omari, Kamel
Nichols, Charles E.
Lockyer, Michael
Lamb, Heather K.
Charles, Ian G.
Hawkins, Alastair R.
Stammers, David K.
Title Structural and functional characterization of Salmonella enterica serovar typhimurium YcbL: an unusual type II glyoxalase
Formatted title
Structural and functional characterization of Salmonella enterica serovar typhimurium YcbL: an unusual type II glyoxalase
Journal name Protein Science   Check publisher's open access policy
ISSN 0961-8368
1469-896X
Publication date 2010-10
Sub-type Article (original research)
DOI 10.1002/pro.475
Open Access Status
Volume 19
Issue 10
Start page 1897
End page 1905
Total pages 9
Place of publication Hoboken, NJ, United States
Publisher Wiley-Blackwell Publishing
Formatted 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.
Keyword β-lactamase
Crystal
Glyoxalase II
Salmonella typhimurium
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Chemistry and Molecular Biosciences
 
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