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dc.contributor.author
Capaldi, Stefano
dc.contributor.author
Faggion, Beniamino
dc.contributor.author
Carrizo Garcia, Maria Elena
dc.contributor.author
Destéfanis, María Laura
dc.contributor.author
Gonzalez, Maria C.
dc.contributor.author
Perduca, Massimiliano
dc.contributor.author
Bovi, Michele
dc.contributor.author
Galliano, Monica
dc.contributor.author
Monaco, Hugo
dc.date.available
2018-03-05T19:43:51Z
dc.date.issued
2015-05
dc.identifier.citation
Capaldi, Stefano; Faggion, Beniamino; Carrizo Garcia, Maria Elena; Destéfanis, María Laura; Gonzalez, Maria C.; et al.; Three-dimensional structure and ligand-binding site of carp fishelectin (FEL); International Union of Crystallography; Acta Crystallographica Section D-Biological Crystallography; 71; 5; 5-2015; 1123-1135
dc.identifier.issn
0907-4449
dc.identifier.uri
http://hdl.handle.net/11336/37888
dc.description.abstract
Carp FEL (fishelectin or fish-egg lectin) is a 238-amino-acid lectin that can be purified from fish eggs by exploiting its selective binding to Sepharose followed by elution with N-acetylglucosamine. Its amino-acid sequence and other biochemical properties have previously been reported. The glycoprotein has four disulfide bridges and the structure of the oligosaccharides linked to Asn27 has been described. Here, the three-dimensional structures of apo carp FEL (cFEL) and of its complex with N-acetylglucosamine determined by X-ray crystallography at resolutions of 1.35 and 1.70Å, respectively, are reported. The molecule folds as a six-bladed β-propeller and internal short consensus amino-acid sequences have been identified in all of the blades. A calcium atom binds at the bottom of the funnel-shaped tunnel located in the centre of the propeller. Two ligand-binding sites, and β, are present in each of the two protomers in the dimer. The first site, , is closer to the N-terminus of the chain and is located in the crevice between the second and the third blades, while the second site, β, is located between the fourth and the fifth blades. The amino acids that participate in the contacts have been identified, as well as the conserved water molecules in all of the sites. Both sites can bind the two anomers, and β, of N-acetylglucosamine, as is clearly recognizable in the electron-density maps. The lectin presents sequence homology to members of the tachylectin family, which are known to have a function in the innate immune system of arthropods, and homologous genes are present in the genomes of other fish and amphibians. This structure is the first of a protein of this group and, given the degree of homology with other members of the family, it is expected that it will be useful to experimentally determine other crystal structures using the coordinates of cFEL as a search probe in molecular replacement.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
International Union of Crystallography
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Fish-Egg Lectin
dc.subject
Fishelectin
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Tachylectins
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Β-Propeller
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Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Three-dimensional structure and ligand-binding site of carp fishelectin (FEL)
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-03-02T14:17:42Z
dc.identifier.eissn
1399-0047
dc.journal.volume
71
dc.journal.number
5
dc.journal.pagination
1123-1135
dc.journal.pais
Reino Unido
dc.journal.ciudad
Chester
dc.description.fil
Fil: Capaldi, Stefano. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
dc.description.fil
Fil: Faggion, Beniamino. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
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Fil: Carrizo Garcia, Maria Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Química Biológica; Argentina
dc.description.fil
Fil: Destéfanis, María Laura. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
dc.description.fil
Fil: Gonzalez, Maria C.. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
dc.description.fil
Fil: Perduca, Massimiliano. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
dc.description.fil
Fil: Bovi, Michele. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
dc.description.fil
Fil: Galliano, Monica. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
dc.description.fil
Fil: Monaco, Hugo. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
dc.journal.title
Acta Crystallographica Section D-Biological Crystallography
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1107/S1399004715004174
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://scripts.iucr.org/cgi-bin/paper?S1399004715004174
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