5K8E
Xylooligosaccharide oxidase from Myceliophthora thermophila C1
Summary for 5K8E
| Entry DOI | 10.2210/pdb5k8e/pdb |
| Descriptor | FAD linked oxidase-like protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, FLAVIN-ADENINE DINUCLEOTIDE, ... (7 entities in total) |
| Functional Keywords | fad, cazy, oligosaccharide, xylose, xylan, oxidoreductase |
| Biological source | Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) |
| Total number of polymer chains | 1 |
| Total formula weight | 57145.98 |
| Authors | Rozeboom, H.J.,Ferrari, A.R.,Fraaije, M.W. (deposition date: 2016-05-30, release date: 2016-09-21, Last modification date: 2024-11-06) |
| Primary citation | Ferrari, A.R.,Rozeboom, H.J.,Dobruchowska, J.M.,van Leeuwen, S.S.,Vugts, A.S.,Koetsier, M.J.,Visser, J.,Fraaije, M.W. Discovery of a Xylooligosaccharide Oxidase from Myceliophthora thermophila C1. J.Biol.Chem., 291:23709-23718, 2016 Cited by PubMed Abstract: By inspection of the predicted proteome of the fungus Myceliophthora thermophila C1 for vanillyl-alcohol oxidase (VAO)-type flavoprotein oxidases, a putative oligosaccharide oxidase was identified. By homologous expression and subsequent purification, the respective protein could be obtained. The protein was found to contain a bicovalently bound FAD cofactor. By screening a large number of carbohydrates, several mono- and oligosaccharides could be identified as substrates. The enzyme exhibits a strong substrate preference toward xylooligosaccharides; hence it is named xylooligosaccharide oxidase (XylO). Chemical analyses of the product formed upon oxidation of xylobiose revealed that the oxidation occurs at C1, yielding xylobionate as product. By elucidation of several XylO crystal structures (in complex with a substrate mimic, xylose, and xylobiose), the residues that tune the unique substrate specificity and regioselectivity could be identified. The discovery of this novel oligosaccharide oxidase reveals that the VAO-type flavoprotein family harbors oxidases tuned for specific oligosaccharides. The unique substrate profile of XylO hints at a role in the degradation of xylan-derived oligosaccharides by the fungus M. thermophila C1. PubMed: 27629413DOI: 10.1074/jbc.M116.741173 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.93 Å) |
Structure validation
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