The crystal structure of acidic β-galactosidase from Aspergillus oryzae.

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.

DOI: 10.1016/j.ijbiomac.2013.05.003

Cite this paper

@article{Maksimainen2013TheCS, title={The crystal structure of acidic β-galactosidase from Aspergillus oryzae.}, author={Mirko M Maksimainen and Anja Lampio and Mirka Mertanen and Ossi Turunen and Juha Rouvinen}, journal={International journal of biological macromolecules}, year={2013}, volume={60}, pages={109-15} }