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1uas

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Image:1uas.jpg

1uas, resolution 1.50Å

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Crystal structure of rice alpha-galactosidase

Overview

alpha-Galactosidases catalyze the hydrolysis of alpha-1,6-linked, galactosyl residues from galacto-oligosaccharides and polymeric, galacto-(gluco)mannans. The crystal structure of rice alpha-galactosidase, has been determined at 1.5A resolution using the multiple isomorphous, replacement method. The structure consisted of a catalytic domain and a, C-terminal domain and was essentially the same as that of, alpha-N-acetylgalactosaminidase, which is the same member of glycosyl, hydrolase family 27. The catalytic domain had a (beta/alpha)8-barrel, structure, and the C-terminal domain was made up of eight beta-strands, containing a Greek key motif. The structure was solved as a complex with, d-galactose, providing a mode of substrate binding in detail. The, d-galactose molecule was found bound in the active site pocket on the, C-terminal side of the central beta-barrel of the catalytic domain. The, d-galactose molecule consisted of a mixture of two anomers present in a, ratio equal to their natural abundance. Structural comparisons of rice, alpha-galactosidase with chicken alpha-N-acetylgalactosaminidase provided, further understanding of the substrate recognition mechanism in these, enzymes.

About this Structure

1UAS is a Single protein structure of sequence from Oryza sativa with GLA, SO4, PT and GOL as ligands. Active as Alpha-galactosidase, with EC number 3.2.1.22 Full crystallographic information is available from OCA.

Reference

Crystal structure of rice alpha-galactosidase complexed with D-galactose., Fujimoto Z, Kaneko S, Momma M, Kobayashi H, Mizuno H, J Biol Chem. 2003 May 30;278(22):20313-8. Epub 2003 Mar 25. PMID:12657636

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