5c86 | pdb_00005c86

Novel fungal alcohol oxidase with catalytic diversity among the AA5 family, apo form

spinqualitylabelsall models 5c86, resolution 1.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5c86 is a 1 chain structure with sequence from Colletotrichum graminicola M1.001. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E3QHV8_COLGM Publication Abstract from PubMed 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-a-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. Structure-function characterization reveals new catalytic diversity in the galactose oxidase and glyoxal oxidase family.,Yin DT, Urresti S, Lafond M, Johnston EM, Derikvand F, Ciano L, Berrin JG, Henrissat B, Walton PH, Davies GJ, Brumer H Nat Commun. 2015 Dec 18;6:10197. doi: 10.1038/ncomms10197. PMID:26680532 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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