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Structure of the putative mutarotase YeaD from Salmonella typhimurium in two different forms: in vivo binding of a sugar phosphate

Chittori, Sagar and Simanshu, Dhirendra K and Savithri, HS and Murthy, MRN (2007) Structure of the putative mutarotase YeaD from Salmonella typhimurium in two different forms: in vivo binding of a sugar phosphate. In: Acta Crystallographica Section D Biological Crystallography, 63 (2). pp. 197-205.

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Abstract

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 angstrom resolution and in a monoclinic form at 2.5 angstrom 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.
Keywords: Salmonella typhimurium; carbohydrates; aldose 1-epimerases; mutarotases; YeaD; GalM; sugar phosphates.
Department/Centre: Division of Biological Sciences > Biochemistry
Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 14 Dec 2010 06:36
Last Modified: 14 Dec 2010 06:36
URI: http://eprints.iisc.ernet.in/id/eprint/34009

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