1. Academic Validation
  2. Crystal Structure of α-Xylosidase from Aspergillus niger in Complex with a Hydrolyzed Xyloglucan Product and New Insights in Accurately Predicting Substrate Specificities of GH31 Family Glycosidases

Crystal Structure of α-Xylosidase from Aspergillus niger in Complex with a Hydrolyzed Xyloglucan Product and New Insights in Accurately Predicting Substrate Specificities of GH31 Family Glycosidases

  • ACS Sustain Chem Eng. 2020 Feb 17;8(6):2540-2547. doi: 10.1021/acssuschemeng.9b07073.
Hongnan Cao 1 2 Jonathan D Walton 3 Phillip Brumm 4 George N Phillips Jr 1 2
Affiliations

Affiliations

  • 1 BioSciences at Rice and Department of Chemistry, Rice University, Houston, Texas 77251, United States.
  • 2 Great Lakes Bioenergy Research Center and Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, United States.
  • 3 Great Lakes Bioenergy Research Center and Department of Plant Biology, Michigan State University, East Lansing, Michigan 48824, United States.
  • 4 C5-6 Technologies Corp., Middleton, Wisconsin 53562, United States.
Abstract

Glycoside hydrolase family 31 (GH31) Enzymes show both highly conserved folds and catalytic residues. Yet different members of GH31 show very different substrate specificities, and it is not obvious how these specificities arise from the protein sequences. The Fungal α-xylosidase, AxlA, was originally isolated from a commercial Enzyme mixture secreted by Aspergillus niger and was reported to have potential as a catalytic component in biomass deconstruction in the biofuel industry. We report here the crystal structure of AxlA in complex with its catalytic product, a hydrolyzed xyloglucan oligosaccharide. On the basis of our new structure, we provide the structural basis for AxlA's role in xyloglucan utilization and, more importantly, a new procedure to predict and differentiate C5 vs C6 sugar specific activities based on protein sequences of the functionally diverse GH31 family Enzymes.

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