Structural characterization of the nonameric assembly of an Archaeal alpha-L-fucosidase by synchrotron small angle X-ray scattering |
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Authors: | Rosano Camillo Zuccotti Simone Cobucci-Ponzano Beatrice Mazzone Marialuisa Rossi Mosè Moracci Marco Petoukhov Maxim V Svergun Dmitri I Bolognesi Martino |
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Institution: | X-ray Structural Biology Unit--National Institute for Cancer Research (IST), Largo R. Benzi 10, 16132 Genoa, Italy. |
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Abstract: | alpha-l-Fucosidase is a lysosomal enzyme responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of carbohydrate moieties in glycoproteins. The first alpha-l-fucosidase from Archaea was recently identified in the genome of the hyperthermophile Sulfolobus solfataricus; the enzyme is encoded by two open reading frames separated by a -1 frameshift. A preliminary biochemical and biophysical characterization of this extremophile enzyme has been carried out both in solution, through small angle X-ray scattering experiments, and in the crystalline state, showing an unusual oligomeric assembly resulting from the association of nine subunits, endowed with 3-fold molecular symmetry. |
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