Structural characterization of the nonameric assembly of an Archaeal α-L-fucosidase by synchrotron small angle X-ray scattering

Camillo Rosano, Simone Zuccotti, Beatrice Cobucci-Ponzano, Marialuisa Mazzone, Mosè Rossi, Marco Moracci, Maxim V. Petoukhov, Dmitri I. Svergun, Martino Bolognesi

Research output: Contribution to journalArticle

Abstract

α-L-Fucosidase is a lysosomal enzyme responsible for hydrolyzing the α-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of carbohydrate moieties in glycoproteins. The first α-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.

Original languageEnglish
Pages (from-to)176-182
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume320
Issue number1
DOIs
Publication statusPublished - Jul 16 2004

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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