The crystal structure of acidic ¦Â-galactosidase from Aspergillus oryzae

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• 作者：Mirko M. Maksimainen ; Anja Lampio ; Mirka Mertanen ; Ossi Turunen ; Juha Rouvinen
• 关键词：PDB ; Protein Data Bank ; Ao-¦Â-gal ; ¦Â-galactosidase from Aspergillus oryzae ; Psp-¦Â-gal ; ¦Â-galactosidase from Penicllium sp. ; Tr-¦Â-gal ; ¦Â-galactosidase from Trichoderma reesei ; MPD ; 2-methyl-2 ; 4-pentanediol
• 刊名：International Journal of Biological Macromolecules
• 出版年：2013
• 出版时间：September, 2013
• 年：2013
• 卷：60
• 期：Complete
• 页码：109-115
• 全文大小：3751 K

文摘

The crystal structure of the industrially important Aspergillus oryzae ¦Â-galactosidase has been determined at 2.60 ? resolution. The Ao-¦Â-gal is a large (985 residues) monomeric multi-domain enzyme that has a catalytic (¦Á/¦Â)8-barrel domain. An electron density map revealed extensive N-glycosylation between the domain interfaces suggesting that the oligosaccharide-chains would have a stabilizing role for the structure of Ao-¦Â-gal. Comparison of structure with other ¦Â-galactosidase structures of glycoside hydrolase family 35 revealed a number of hydrophobic residues, which may contribute favorably to the stabilization of the structure. The role of a high number of acidic residues in Ao-¦Â-gal is also discussed.