Structural characterization of the nonameric assembly of an Archaeal alpha-L-fucosidase by synchrotron small angle X-ray scattering.
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.
Rosano
Camillo
C
X-ray Structural Biology Unit--National Institute for Cancer Research (IST), Largo R. Benzi 10, 16132 Genoa, Italy.
Zuccotti
Simone
S
Cobucci-Ponzano
Beatrice
B
Mazzone
Marialuisa
M
Rossi
Mosè
M
Moracci
Marco
M
Petoukhov
Maxim V
MV
Svergun
Dmitri I
DI
Bolognesi
Martino
M
D003198:Computer Simulation; D003460:Crystallization / Q000379:methods*; D008958:Models, Molecular; D008970:Molecular Weight; D011487:Protein Conformation; D020836:Protein Structure, Quaternary; D012996:Solutions; D016944:Sulfolobus / Q000201:enzymology*; D017356:Synchrotrons; D014961:X-Ray Diffraction / Q000379:methods*; D005644:alpha-L-Fucosidase / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism
D012996:Solutions; D005644:alpha-L-Fucosidase