http://www.cnr.it/ontology/cnr/individuo/prodotto/ID8745
Structural characterization of the nonameric assembly of an Archaeal alpha-L-fucosidase by synchrotron small angle X-ray scattering (Articolo in rivista)
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- Structural characterization of the nonameric assembly of an Archaeal alpha-L-fucosidase by synchrotron small angle X-ray scattering (Articolo in rivista) (literal)
- Anno
- 2004-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.bbrc.2004.05.149 (literal)
- Alternative label
Rosano C., Zuccotti S.; Cobucci-Ponzano B.; Mazzone M.; Rossi M.; Moracci M., Petoukhov M.V.; Svergun D.I.; Bolognesi M. (2004)
Structural characterization of the nonameric assembly of an Archaeal alpha-L-fucosidase by synchrotron small angle X-ray scattering
in Biochemical and biophysical research communications (Print); Academic Press Elsevier, Inc., San Diego (Stati Uniti d'America)
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- Rosano C., Zuccotti S.; Cobucci-Ponzano B.; Mazzone M.; Rossi M.; Moracci M., Petoukhov M.V.; Svergun D.I.; Bolognesi M. (literal)
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- X-ray Structural Biology Unit--National Institute for Cancer Research (IST), Largo R. Benzi 10, 16132 Genoa, Italy
Department of Physics INFM and Center of Excellence for Biomedical Research, University of Genova, Via Dodecaneso 33, 16146 Genoa, Italy
Institute of Protein Biochemistry--Consiglio Nazionale delle Ricerche, Via P. Castellino 111, 80131 Naples, Italy
Dipartimento di Chimica Biologica, Università di Napoli \"Federico II\", Via Mezzocannone 16, 80134 Naples, Italy
European Molecular Biology Laboratory, Hamburg Outstation, EMBL c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany
Institute of Crystallography, Russian Academy of Sciences, Leninsky pr. 59, 117333 Moscow, Russia (literal)
- Titolo
- Structural characterization of the nonameric assembly of an Archaeal alpha-L-fucosidase by synchrotron small angle X-ray scattering (literal)
- 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. (literal)
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