Structure of the putative mutarotase YeaD from Salmonella typhimurium: structural comparison with galactose mutarotases.
Salmonella typhimurium YeaD (stYeaD), annotated as a putative aldose 1-epimerase, has a very low sequence identity to other well characterized mutarotases. Sequence analysis suggested that the catalytic residues and a few of the substrate-binding residues of galactose mutarotases (GalMs) are conserved in stYeaD. Determination of the crystal structure of stYeaD in an orthorhombic form at 1.9 A resolution and in a monoclinic form at 2.5 A resolution revealed this protein to adopt the beta-sandwich fold similar to GalMs. Structural comparison of stYeaD with GalMs has permitted the identification of residues involved in catalysis and substrate binding. In spite of the similar fold and conservation of catalytic residues, minor but significant differences were observed in the substrate-binding pocket. These analyses pointed out the possible role of Arg74 and Arg99, found only in YeaD-like proteins, in ligand anchoring and suggested that the specificity of stYeaD may be distinct from those of GalMs.
Chittori
Sagar
S
Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Simanshu
Dhirendra K
DK
Savithri
H S
HS
Murthy
M R N
MR
D001120:Arginine; D001426:Bacterial Proteins / Q000737:chemistry; D001665:Binding Sites; D002238:Carbohydrate Epimerases / Q000737:chemistry*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D008024:Ligands; D015394:Molecular Structure; D011487:Protein Conformation; D012486:Salmonella typhimurium / Q000201:enzymology*; D013379:Substrate Specificity
D001426:Bacterial Proteins; D008024:Ligands; D001120:Arginine; D002238:Carbohydrate Epimerases; C019646:aldose 1-epimerase; C459183:galactose mutarotase