2hta

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

spinqualitylabelsall models 2hta, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2hta is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, SO4 Related: 1jov, 1l7k, 1z45, 1lur, 1snz Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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