5C92
Novel fungal alcohol oxidase with catalytic diversity among the AA5 family, in complex with copper
Summary for 5C92
| Entry DOI | 10.2210/pdb5c92/pdb |
| Descriptor | Kelch domain-containing protein, 2-acetamido-2-deoxy-beta-D-glucopyranose, COPPER (I) ION, ... (5 entities in total) |
| Functional Keywords | kelch motif, aa5, fungal alcohol oxidase, oxidoreductase |
| Biological source | Colletotrichum graminicola M1.001 (Maize anthracnose fungus) |
| Total number of polymer chains | 1 |
| Total formula weight | 52951.69 |
| Authors | Urresti, S.,Yin, D.T.,LaFond, M.,Derikvand, F.,Berrin, G.J.,Henrissat, B.,Walton, P.H.,Brumer, H.,Davies, G.J. (deposition date: 2015-06-26, release date: 2015-07-08, Last modification date: 2024-01-10) |
| Primary citation | Yin, D.T.,Urresti, S.,Lafond, M.,Johnston, E.M.,Derikvand, F.,Ciano, L.,Berrin, J.G.,Henrissat, B.,Walton, P.H.,Davies, G.J.,Brumer, H. Structure-function characterization reveals new catalytic diversity in the galactose oxidase and glyoxal oxidase family. Nat Commun, 6:10197-10197, 2015 Cited by PubMed Abstract: Alcohol oxidases, including carbohydrate oxidases, have a long history of research that has generated fundamental biological understanding and biotechnological applications. Despite a long history of study, the galactose 6-oxidase/glyoxal oxidase family of mononuclear copper-radical oxidases, Auxiliary Activity Family 5 (AA5), is currently represented by only very few characterized members. Here we report the recombinant production and detailed structure-function analyses of two homologues from the phytopathogenic fungi Colletotrichum graminicola and C. gloeosporioides, CgrAlcOx and CglAlcOx, respectively, to explore the wider biocatalytic potential in AA5. EPR spectroscopy and crystallographic analysis confirm a common active-site structure vis-à-vis the archetypal galactose 6-oxidase from Fusarium graminearum. Strikingly, however, CgrAlcOx and CglAlcOx are essentially incapable of oxidizing galactose and galactosides, but instead efficiently catalyse the oxidation of diverse aliphatic alcohols. The results highlight the significant potential of prospecting the evolutionary diversity of AA5 to reveal novel enzyme specificities, thereby informing both biology and applications. PubMed: 26680532DOI: 10.1038/ncomms10197 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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