Chittori, Sagar and Simanshu, Dhirendra K and Savithri, HS and Murthy, MRN (2007) Structure of the putative mutarotase YeaD from Salmonella typhimurium: structural comparison with galactose mutarotases. In: Acta Crystallographica Section D- Biological Crystallography, 63 (2). pp. 197-205.
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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 \AA resolution and in a monoclinic form at 2.5 \AA 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.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to International Union of Crystallography.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit
Division of Biological Sciences > Biochemistry
|Date Deposited:||21 Mar 2007|
|Last Modified:||19 Sep 2010 04:35|
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