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

Fingerprint

alpha-L-Fucosidase
Synchrotrons
X ray scattering
X-Rays
Enzymes
Sulfolobus solfataricus
Fucose
Acetylglucosamine
Archaea
Open Reading Frames
Glycoproteins
Genes
Carbohydrates
Genome
Crystalline materials
Experiments

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Structural characterization of the nonameric assembly of an Archaeal α-L-fucosidase by synchrotron small angle X-ray scattering. / Rosano, Camillo; Zuccotti, Simone; Cobucci-Ponzano, Beatrice; Mazzone, Marialuisa; Rossi, Mosè; Moracci, Marco; Petoukhov, Maxim V.; Svergun, Dmitri I.; Bolognesi, Martino.

In: Biochemical and Biophysical Research Communications, Vol. 320, No. 1, 16.07.2004, p. 176-182.

Research output: Contribution to journalArticle

Rosano, Camillo ; Zuccotti, Simone ; Cobucci-Ponzano, Beatrice ; Mazzone, Marialuisa ; Rossi, Mosè ; Moracci, Marco ; Petoukhov, Maxim V. ; Svergun, Dmitri I. ; Bolognesi, Martino. / Structural characterization of the nonameric assembly of an Archaeal α-L-fucosidase by synchrotron small angle X-ray scattering. In: Biochemical and Biophysical Research Communications. 2004 ; Vol. 320, No. 1. pp. 176-182.
@article{a309a85a714f4f59a1b81663f7d18c8d,
title = "Structural characterization of the nonameric assembly of an Archaeal α-L-fucosidase by synchrotron small angle X-ray scattering",
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.",
author = "Camillo Rosano and Simone Zuccotti and Beatrice Cobucci-Ponzano and Marialuisa Mazzone and Mos{\`e} Rossi and Marco Moracci and Petoukhov, {Maxim V.} and Svergun, {Dmitri I.} and Martino Bolognesi",
year = "2004",
month = "7",
day = "16",
doi = "10.1016/j.bbrc.2004.05.149",
language = "English",
volume = "320",
pages = "176--182",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Structural characterization of the nonameric assembly of an Archaeal α-L-fucosidase by synchrotron small angle X-ray scattering

AU - Rosano, Camillo

AU - Zuccotti, Simone

AU - Cobucci-Ponzano, Beatrice

AU - Mazzone, Marialuisa

AU - Rossi, Mosè

AU - Moracci, Marco

AU - Petoukhov, Maxim V.

AU - Svergun, Dmitri I.

AU - Bolognesi, Martino

PY - 2004/7/16

Y1 - 2004/7/16

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=2942689211&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=2942689211&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2004.05.149

DO - 10.1016/j.bbrc.2004.05.149

M3 - Article

C2 - 15207718

AN - SCOPUS:2942689211

VL - 320

SP - 176

EP - 182

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -