4IUG

Crystal structure of beta-galactosidase from Aspergillus oryzae in complex with galactose

4IUG の概要

• エントリーDOI: 10.2210/pdb4iug/pdb
• 分子名称: Beta-galactosidase A, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total)
• 機能のキーワード: tim barrel, glycoside hydrolase, hydrolase
• 由来する生物種: Aspergillus oryzae (Yellow koji mold)
• 細胞内の位置: Secreted (By similarity): Q2UCU3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 120151.36

構造登録者

Maksimainen, M.,Rouvinen, J. (登録日: 2013-01-21, 公開日: 2013-07-31, 最終更新日: 2024-11-20)

主引用文献

Maksimainen, M.M.,Lampio, A.,Mertanen, M.,Turunen, O.,Rouvinen, J.
The crystal structure of acidic beta-galactosidase from Aspergillus oryzae.
Int.J.Biol.Macromol., 60C:109-115, 2013

PubMed Abstract: The crystal structure of the industrially important Aspergillus oryzae β-galactosidase has been determined at 2.60 Å resolution. The Ao-β-gal is a large (985 residues) monomeric multi-domain enzyme that has a catalytic (α/β)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-β-gal. Comparison of structure with other β-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-β-gal is also discussed.

PubMed: 23688418
DOI: 10.1016/j.ijbiomac.2013.05.003

実験手法

X-RAY DIFFRACTION (2.6 Å)