1UAS

Crystal structure of rice alpha-galactosidase

Summary for 1UAS

• Entry DOI: 10.2210/pdb1uas/pdb
• Descriptor: alpha-galactosidase, alpha-D-galactopyranose, SULFATE ION, ... (6 entities in total)
• Functional Keywords: tim-barrel, beta-alpha-barrel, greek key motif, hydrolase
• Biological source: Oryza sativa (rice)
• Total number of polymer chains: 1
• Total formula weight: 41105.23

Authors

Fujimoto, Z.,Kaneko, S.,Momma, M.,Kobayashi, H.,Mizuno, H. (deposition date: 2003-03-18, release date: 2003-07-01, Last modification date: 2024-10-30)

Primary citation

Fujimoto, Z.,Kaneko, S.,Momma, M.,Kobayashi, H.,Mizuno, H.
Crystal structure of rice alpha-galactosidase complexed with D-galactose
J.Biol.Chem., 278:20313-20318, 2003

PubMed Abstract: 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.

PubMed: 12657636
DOI: 10.1074/jbc.M302292200

Experimental method

X-RAY DIFFRACTION (1.5 Å)