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PMID:21192932
| Citation |
Lee, SJ, Kim, HS, Kim, do J, Yoon, HJ, Kim, KH, Yoon, JY and Suh, SW (2011) Crystal structures of LacD from Staphylococcus aureus and LacD.1 from Streptococcus pyogenes: insights into substrate specificity and virulence gene regulation. FEBS Lett. 585:307-12 |
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| Abstract |
Staphylococcus aureus LacD, a Class I tagatose-1,6-bisphosphate (TBP) aldolase, shows broadened substrate specificity by catalyzing the cleavage of 1,6-bisphosphate derivatives of D-tagatose, D-fructose, D-sorbose, and D-psicose. LacD.1 and LacD.2 are two closely-related Class I TBP aldolases in Streptococcus pyogenes. Here we have determined the crystal structures of S. aureus LacD and S. pyogenes LacD.1. Monomers of both enzymes are folded into a (β/α)(8) barrel and two monomers associate tightly to form a dimer in the crystals. The structures suggest that the residues E189 and S300 of rabbit muscle Class I fructose-1,6-bisphosphate (FBP) aldolase are important for substrate specificity. When we mutated the corresponding residues of S. aureus LacD, the mutants (L165E, L275S, and L165E/L275S) showed enhanced substrate specificity toward FBP. |
| Links |
PubMed Online version:10.1016/j.febslet.2010.12.038 |
| Keywords |
Aldehyde-Lyases/chemistry; Bacterial Proteins/chemistry; Crystallography, X-Ray; Mutation, Missense; Staphylococcus aureus/enzymology; Streptococcus pyogenes/enzymology; Substrate Specificity; Virulence/genetics |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0009025: tagatose-bisphosphate aldolase activity |
ECO:0000269: |
F |
Crystal structures of LacD from Staphylococcus aureus and LacD.1 from Streptococcus pyogenes: insights into substrate specificity and virulence gene regulation.Crystal structures of LacD from Staphylococcus aureus and LacD.1 from Streptococcus pyogenes: insights into substrate specificity and virulence gene regulation. |
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