4IUG

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

Summary for 4IUG

• Entry DOI: 10.2210/pdb4iug/pdb
• Descriptor: 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)
• Functional Keywords: tim barrel, glycoside hydrolase, hydrolase
• Biological source: Aspergillus oryzae (Yellow koji mold)
• Cellular location: Secreted (By similarity): Q2UCU3
• Total number of polymer chains: 1
• Total formula weight: 120151.36

Authors

Maksimainen, M.,Rouvinen, J. (deposition date: 2013-01-21, release date: 2013-07-31, Last modification date: 2023-09-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)