6DRU
Xylosidase from Aspergillus niger
Summary for 6DRU
| Entry DOI | 10.2210/pdb6dru/pdb |
| Descriptor | Glycosyl hydrolases family 31 family protein, GLYCEROL, alpha-D-mannopyranose-(1-2)-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, ... (11 entities in total) |
| Functional Keywords | alpha-xylosidase, structural genomics, psi-2, protein structure initiative, enzyme discovery for natural product biosynthesis, natpro, hydrolase |
| Biological source | Aspergillus niger |
| Total number of polymer chains | 2 |
| Total formula weight | 173961.55 |
| Authors | Cao, H.,Xu, W.,Betancourt, M.,Walton, J.D.,Brumm, P.,Phillips Jr., G.N.,Enzyme Discovery for Natural Product Biosynthesis (NatPro) (deposition date: 2018-06-13, release date: 2018-08-22, Last modification date: 2024-11-13) |
| Primary citation | Cao, H.,Walton, J.D.,Brumm, P.,Phillips Jr., G.N. Crystal Structure of alpha-Xylosidase fromAspergillus nigerin Complex with a Hydrolyzed Xyloglucan Product and New Insights in Accurately Predicting Substrate Specificities of GH31 Family Glycosidases. Acs Sustain Chem Eng, 8:2540-2547, 2020 Cited by PubMed 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 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. PubMed: 32161692DOI: 10.1021/acssuschemeng.9b07073 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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