Structure of Aspergillus aculeatus β-1,4-galactanase in complex with galactobiose

Acta Crystallogr F Struct Biol Commun. 2019 Jun 1;75(Pt 6):399-404. doi: 10.1107/S2053230X19005612. Epub 2019 May 10.

Abstract

β-1,4-Galactanases are glycoside hydrolases that are involved in the degradation of pectin and belong to family 53 in the classification of glycoside hydrolases. Previous studies have elucidated the structures of several fungal and two bacterial galactanases, while biochemical studies have indicated differences in the product profiles of different members of the family. Structural studies of ligand complexes have to date been limited to the bacterial members of the family. Here, the first structure of a fungal galactanase in complex with a disaccharide is presented. Galactobiose binds to subsites -1 and -2, thus improving our understanding of ligand binding to galactanases.

Keywords: Aspergillus aculeatus; glycoside hydrolases; oligosaccharides; pectin; specificity; β-1,4-galactanases.

MeSH terms

  • Aspergillus / enzymology*
  • Crystallography, X-Ray
  • Disaccharides / chemistry*
  • Disaccharides / metabolism*
  • Glycoside Hydrolases / chemistry*
  • Glycoside Hydrolases / metabolism*
  • Models, Molecular*
  • Protein Conformation
  • Substrate Specificity

Substances

  • Disaccharides
  • 6-O-galactopyranosylgalactose
  • Glycoside Hydrolases
  • arabinogalactan endo-1,4-beta-galactosidase