Structure and properties of the giant reed (Arundo donax) lectin (ADL)

Autores
Perduca, Massimiliano; Bovi, Michele; Destefanis, Laura; Nadali, Divina; Fin, Laura; Parolini, Francesca; Sorio, Daniela; Carrizo Garcia, Maria Elena; Monaco, Hugo
Año de publicación
2021
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Arundo donax lectin (ADL) is a 170 amino acid protein that can be purified from the rhizomes of the giant reed or giant cane by exploiting its selective binding to chitin followed by elution with N-acetylglucosamine. The lectin is listed in the UniProt server, the largest protein sequence database, as an uncharacterized protein with chitin-binding domains (A0A0A9P802). This paper reports the purification, structure and ligand-binding properties of ADL. The lectin is a homodimer in which the two protomers are linked by two disulfide bridges. Each polypeptide chain presents four carbohydrate-binding modules that belong to carbohydrate-binding module family 18. A high degree of sequence similarity is observed among the modules present in each protomer. We have determined the X-ray structure of the apo-protein to a resolution of 1.70 Å. The carbohydrate-binding modules, that span a sequence of approximately 40 amino acids, present four internal disulfide bridges, a very short antiparallel central beta sheet and three short alpha helices, two on one side of the beta sheet and one on the other. The structures of the complexes of the lectin with N-acetylglucosamine, N-acetyllactosamine, N-acetylneuraminic acid and N-N'diacetylchitobiose reveal that ADL has two primary and two secondary carbohydrate-binding sites per dimer. They are located at the interface between the two protomers, and each binding site involves residues of both chains. The lectin presents structural similarity to the wheat germ agglutinin family, in particular, to isoform 3.
Fil: Perduca, Massimiliano. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
Fil: Bovi, Michele. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
Fil: Destefanis, Laura. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
Fil: Nadali, Divina. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
Fil: Fin, Laura. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
Fil: Parolini, Francesca. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
Fil: Sorio, Daniela. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
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
Fil: Monaco, Hugo. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
Materia
ARUNDO DONAX LECTIN
N-ACETYLGLUCOSAMINE
N-ACETYLLACTOSAMINE
N-ACETYLNEURAMINIC ACID
N′ DIACETYLCHITOBIOSE
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/195488
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/195488
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Structure and properties of the giant reed (Arundo donax) lectin (ADL)Perduca, MassimilianoBovi, MicheleDestefanis, LauraNadali, DivinaFin, LauraParolini, FrancescaSorio, DanielaCarrizo Garcia, Maria ElenaMonaco, HugoARUNDO DONAX LECTINN-ACETYLGLUCOSAMINEN-ACETYLLACTOSAMINEN-ACETYLNEURAMINIC ACIDN′ DIACETYLCHITOBIOSEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Arundo donax lectin (ADL) is a 170 amino acid protein that can be purified from the rhizomes of the giant reed or giant cane by exploiting its selective binding to chitin followed by elution with N-acetylglucosamine. The lectin is listed in the UniProt server, the largest protein sequence database, as an uncharacterized protein with chitin-binding domains (A0A0A9P802). This paper reports the purification, structure and ligand-binding properties of ADL. The lectin is a homodimer in which the two protomers are linked by two disulfide bridges. Each polypeptide chain presents four carbohydrate-binding modules that belong to carbohydrate-binding module family 18. A high degree of sequence similarity is observed among the modules present in each protomer. We have determined the X-ray structure of the apo-protein to a resolution of 1.70 Å. The carbohydrate-binding modules, that span a sequence of approximately 40 amino acids, present four internal disulfide bridges, a very short antiparallel central beta sheet and three short alpha helices, two on one side of the beta sheet and one on the other. The structures of the complexes of the lectin with N-acetylglucosamine, N-acetyllactosamine, N-acetylneuraminic acid and N-N'diacetylchitobiose reveal that ADL has two primary and two secondary carbohydrate-binding sites per dimer. They are located at the interface between the two protomers, and each binding site involves residues of both chains. The lectin presents structural similarity to the wheat germ agglutinin family, in particular, to isoform 3.Fil: Perduca, Massimiliano. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; ItaliaFil: Bovi, Michele. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; ItaliaFil: Destefanis, Laura. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; ItaliaFil: Nadali, Divina. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; ItaliaFil: Fin, Laura. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; ItaliaFil: Parolini, Francesca. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; ItaliaFil: Sorio, Daniela. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; ItaliaFil: 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; ArgentinaFil: Monaco, Hugo. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; ItaliaOxford Univ Press Inc2021-06-29info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/195488Perduca, Massimiliano; Bovi, Michele; Destefanis, Laura; Nadali, Divina; Fin, Laura; et al.; Structure and properties of the giant reed (Arundo donax) lectin (ADL); Oxford Univ Press Inc; Glycobiology; 31; 11; 29-6-2021; 1543-15560959-66581460-2423CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/glycob/advance-article/doi/10.1093/glycob/cwab059/6311232info:eu-repo/semantics/altIdentifier/doi/10.1093/glycob/cwab059info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:21:43Zoai:ri.conicet.gov.ar:11336/195488instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:21:43.914CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Structure and properties of the giant reed (Arundo donax) lectin (ADL)
title Structure and properties of the giant reed (Arundo donax) lectin (ADL)
spellingShingle Structure and properties of the giant reed (Arundo donax) lectin (ADL)
Perduca, Massimiliano
ARUNDO DONAX LECTIN
N-ACETYLGLUCOSAMINE
N-ACETYLLACTOSAMINE
N-ACETYLNEURAMINIC ACID
N′ DIACETYLCHITOBIOSE
title_short Structure and properties of the giant reed (Arundo donax) lectin (ADL)
title_full Structure and properties of the giant reed (Arundo donax) lectin (ADL)
title_fullStr Structure and properties of the giant reed (Arundo donax) lectin (ADL)
title_full_unstemmed Structure and properties of the giant reed (Arundo donax) lectin (ADL)
title_sort Structure and properties of the giant reed (Arundo donax) lectin (ADL)
dc.creator.none.fl_str_mv Perduca, Massimiliano
Bovi, Michele
Destefanis, Laura
Nadali, Divina
Fin, Laura
Parolini, Francesca
Sorio, Daniela
Carrizo Garcia, Maria Elena
Monaco, Hugo
author Perduca, Massimiliano
author_facet Perduca, Massimiliano
Bovi, Michele
Destefanis, Laura
Nadali, Divina
Fin, Laura
Parolini, Francesca
Sorio, Daniela
Carrizo Garcia, Maria Elena
Monaco, Hugo
author_role author
author2 Bovi, Michele
Destefanis, Laura
Nadali, Divina
Fin, Laura
Parolini, Francesca
Sorio, Daniela
Carrizo Garcia, Maria Elena
Monaco, Hugo
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv ARUNDO DONAX LECTIN
N-ACETYLGLUCOSAMINE
N-ACETYLLACTOSAMINE
N-ACETYLNEURAMINIC ACID
N′ DIACETYLCHITOBIOSE
topic ARUNDO DONAX LECTIN
N-ACETYLGLUCOSAMINE
N-ACETYLLACTOSAMINE
N-ACETYLNEURAMINIC ACID
N′ DIACETYLCHITOBIOSE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Arundo donax lectin (ADL) is a 170 amino acid protein that can be purified from the rhizomes of the giant reed or giant cane by exploiting its selective binding to chitin followed by elution with N-acetylglucosamine. The lectin is listed in the UniProt server, the largest protein sequence database, as an uncharacterized protein with chitin-binding domains (A0A0A9P802). This paper reports the purification, structure and ligand-binding properties of ADL. The lectin is a homodimer in which the two protomers are linked by two disulfide bridges. Each polypeptide chain presents four carbohydrate-binding modules that belong to carbohydrate-binding module family 18. A high degree of sequence similarity is observed among the modules present in each protomer. We have determined the X-ray structure of the apo-protein to a resolution of 1.70 Å. The carbohydrate-binding modules, that span a sequence of approximately 40 amino acids, present four internal disulfide bridges, a very short antiparallel central beta sheet and three short alpha helices, two on one side of the beta sheet and one on the other. The structures of the complexes of the lectin with N-acetylglucosamine, N-acetyllactosamine, N-acetylneuraminic acid and N-N'diacetylchitobiose reveal that ADL has two primary and two secondary carbohydrate-binding sites per dimer. They are located at the interface between the two protomers, and each binding site involves residues of both chains. The lectin presents structural similarity to the wheat germ agglutinin family, in particular, to isoform 3.
Fil: Perduca, Massimiliano. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
Fil: Bovi, Michele. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
Fil: Destefanis, Laura. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
Fil: Nadali, Divina. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
Fil: Fin, Laura. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
Fil: Parolini, Francesca. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
Fil: Sorio, Daniela. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
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
Fil: Monaco, Hugo. Università di Verona. Dipartimento Scientífico e Tecnológico. Laboratorio di Biocristallografia; Italia
description Arundo donax lectin (ADL) is a 170 amino acid protein that can be purified from the rhizomes of the giant reed or giant cane by exploiting its selective binding to chitin followed by elution with N-acetylglucosamine. The lectin is listed in the UniProt server, the largest protein sequence database, as an uncharacterized protein with chitin-binding domains (A0A0A9P802). This paper reports the purification, structure and ligand-binding properties of ADL. The lectin is a homodimer in which the two protomers are linked by two disulfide bridges. Each polypeptide chain presents four carbohydrate-binding modules that belong to carbohydrate-binding module family 18. A high degree of sequence similarity is observed among the modules present in each protomer. We have determined the X-ray structure of the apo-protein to a resolution of 1.70 Å. The carbohydrate-binding modules, that span a sequence of approximately 40 amino acids, present four internal disulfide bridges, a very short antiparallel central beta sheet and three short alpha helices, two on one side of the beta sheet and one on the other. The structures of the complexes of the lectin with N-acetylglucosamine, N-acetyllactosamine, N-acetylneuraminic acid and N-N'diacetylchitobiose reveal that ADL has two primary and two secondary carbohydrate-binding sites per dimer. They are located at the interface between the two protomers, and each binding site involves residues of both chains. The lectin presents structural similarity to the wheat germ agglutinin family, in particular, to isoform 3.
publishDate 2021
dc.date.none.fl_str_mv 2021-06-29
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/195488
Perduca, Massimiliano; Bovi, Michele; Destefanis, Laura; Nadali, Divina; Fin, Laura; et al.; Structure and properties of the giant reed (Arundo donax) lectin (ADL); Oxford Univ Press Inc; Glycobiology; 31; 11; 29-6-2021; 1543-1556
0959-6658
1460-2423
CONICET Digital
CONICET
url http://hdl.handle.net/11336/195488
identifier_str_mv Perduca, Massimiliano; Bovi, Michele; Destefanis, Laura; Nadali, Divina; Fin, Laura; et al.; Structure and properties of the giant reed (Arundo donax) lectin (ADL); Oxford Univ Press Inc; Glycobiology; 31; 11; 29-6-2021; 1543-1556
0959-6658
1460-2423
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/glycob/advance-article/doi/10.1093/glycob/cwab059/6311232
info:eu-repo/semantics/altIdentifier/doi/10.1093/glycob/cwab059
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Oxford Univ Press Inc
publisher.none.fl_str_mv Oxford Univ Press Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 12.982451

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