2htb

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2htb, resolution 2.50Å

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Crystal Structure of a putative mutarotase (YeaD) from Salmonella typhimurium in monoclinic form

Overview

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.

About this Structure

2HTB is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.

Reference

Structure of the putative mutarotase YeaD from Salmonella typhimurium: structural comparison with galactose mutarotases., Chittori S, Simanshu DK, Savithri HS, Murthy MR, Acta Crystallogr D Biol Crystallogr. 2007 Feb;63(Pt 2):197-205. Epub 2007, Jan 16. PMID:17242513

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