Structure of a lectin from Canavalia gladiata seeds: new structural insights for old molecules

Detalhes bibliográficos
Autor(a) principal: Delatorre, Plinio
Data de Publicação: 2007
Outros Autores: Rocha, Bruno A. M., Souza, Emmanuel P., Oliveira, Taiana M., Bezerra, Gustavo A., Moreno, Frederico B. M. B., Freitas, Beatriz T., Santi-Gadelha, Tatiane, Sampaio, Alexandre H., Azevedo, Walter F., Cavada, Benildo S.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1186/1472-6807-7-52
http://hdl.handle.net/11449/31796
Resumo: Background: Lectins are mainly described as simple carbohydrate- binding proteins. Previous studies have tried to identify other binding sites, which possible recognize plant hormones, secondary metabolites, and isolated amino acid residues. We report the crystal structure of a lectin isolated from Canavalia gladiata seeds ( CGL), describing a new binding pocket, which may be related to pathogen resistance activity in ConA- like lectins; a site where a non- protein amino- acid, aaminobutyric acid ( Abu), is bound.Results: the overall structure of native CGL and complexed with alpha- methyl- mannoside and Abu have been refined at 2.3 angstrom and 2.31 angstrom resolution, respectively. Analysis of the electron density maps of the CGL structure shows clearly the presence of Abu, which was confirmed by mass spectrometry.Conclusion: the presence of Abu in a plant lectin structure strongly indicates the ability of lectins on carrying secondary metabolites. Comparison of the amino acids composing the site with other legume lectins revealed that this site is conserved, providing an evidence of the biological relevance of this site. This new action of lectins strengthens their role in defense mechanisms in plants.
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spelling Structure of a lectin from Canavalia gladiata seeds: new structural insights for old moleculesBackground: Lectins are mainly described as simple carbohydrate- binding proteins. Previous studies have tried to identify other binding sites, which possible recognize plant hormones, secondary metabolites, and isolated amino acid residues. We report the crystal structure of a lectin isolated from Canavalia gladiata seeds ( CGL), describing a new binding pocket, which may be related to pathogen resistance activity in ConA- like lectins; a site where a non- protein amino- acid, aaminobutyric acid ( Abu), is bound.Results: the overall structure of native CGL and complexed with alpha- methyl- mannoside and Abu have been refined at 2.3 angstrom and 2.31 angstrom resolution, respectively. Analysis of the electron density maps of the CGL structure shows clearly the presence of Abu, which was confirmed by mass spectrometry.Conclusion: the presence of Abu in a plant lectin structure strongly indicates the ability of lectins on carrying secondary metabolites. Comparison of the amino acids composing the site with other legume lectins revealed that this site is conserved, providing an evidence of the biological relevance of this site. This new action of lectins strengthens their role in defense mechanisms in plants.Univ Fed Ceara, Dept Bioquim & Biol Mol, Ceara, BrazilUniv Reg Cariri, Dept Biol, Ceara, BrazilUniv Fed Paraiba, Dept Biol, Paraiba, BrazilUniv Estadual Paulista, IBILCE, Dept Fis, São Paulo, BrazilPontificia Univ Catolica Rio Grande do Sul, Fac Biociencias, BR-90619900 Porto Alegre, RS, BrazilUniv Estadual Paulista, IBILCE, Dept Fis, São Paulo, BrazilBiomed Central Ltd.Universidade Federal do Ceará (UFC)Univ Reg CaririUniversidade Federal da Paraíba (UFPB)Universidade Estadual Paulista (Unesp)Pontificia Univ Catolica Rio Grande do SulDelatorre, PlinioRocha, Bruno A. M.Souza, Emmanuel P.Oliveira, Taiana M.Bezerra, Gustavo A.Moreno, Frederico B. M. B.Freitas, Beatriz T.Santi-Gadelha, TatianeSampaio, Alexandre H.Azevedo, Walter F.Cavada, Benildo S.2014-05-20T15:20:31Z2014-05-20T15:20:31Z2007-08-02info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article9application/pdfhttp://dx.doi.org/10.1186/1472-6807-7-52Bmc Structural Biology. London: Biomed Central Ltd., v. 7, 9 p., 2007.1471-2237http://hdl.handle.net/11449/3179610.1186/1472-6807-7-52WOS:000249301900001WOS000249301900001.pdfWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengBmc Structural Biologyinfo:eu-repo/semantics/openAccess2023-12-12T06:22:46Zoai:repositorio.unesp.br:11449/31796Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T20:09:50.806059Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Structure of a lectin from Canavalia gladiata seeds: new structural insights for old molecules
title Structure of a lectin from Canavalia gladiata seeds: new structural insights for old molecules
spellingShingle Structure of a lectin from Canavalia gladiata seeds: new structural insights for old molecules
Delatorre, Plinio
title_short Structure of a lectin from Canavalia gladiata seeds: new structural insights for old molecules
title_full Structure of a lectin from Canavalia gladiata seeds: new structural insights for old molecules
title_fullStr Structure of a lectin from Canavalia gladiata seeds: new structural insights for old molecules
title_full_unstemmed Structure of a lectin from Canavalia gladiata seeds: new structural insights for old molecules
title_sort Structure of a lectin from Canavalia gladiata seeds: new structural insights for old molecules
author Delatorre, Plinio
author_facet Delatorre, Plinio
Rocha, Bruno A. M.
Souza, Emmanuel P.
Oliveira, Taiana M.
Bezerra, Gustavo A.
Moreno, Frederico B. M. B.
Freitas, Beatriz T.
Santi-Gadelha, Tatiane
Sampaio, Alexandre H.
Azevedo, Walter F.
Cavada, Benildo S.
author_role author
author2 Rocha, Bruno A. M.
Souza, Emmanuel P.
Oliveira, Taiana M.
Bezerra, Gustavo A.
Moreno, Frederico B. M. B.
Freitas, Beatriz T.
Santi-Gadelha, Tatiane
Sampaio, Alexandre H.
Azevedo, Walter F.
Cavada, Benildo S.
author2_role author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade Federal do Ceará (UFC)
Univ Reg Cariri
Universidade Federal da Paraíba (UFPB)
Universidade Estadual Paulista (Unesp)
Pontificia Univ Catolica Rio Grande do Sul
dc.contributor.author.fl_str_mv Delatorre, Plinio
Rocha, Bruno A. M.
Souza, Emmanuel P.
Oliveira, Taiana M.
Bezerra, Gustavo A.
Moreno, Frederico B. M. B.
Freitas, Beatriz T.
Santi-Gadelha, Tatiane
Sampaio, Alexandre H.
Azevedo, Walter F.
Cavada, Benildo S.
description Background: Lectins are mainly described as simple carbohydrate- binding proteins. Previous studies have tried to identify other binding sites, which possible recognize plant hormones, secondary metabolites, and isolated amino acid residues. We report the crystal structure of a lectin isolated from Canavalia gladiata seeds ( CGL), describing a new binding pocket, which may be related to pathogen resistance activity in ConA- like lectins; a site where a non- protein amino- acid, aaminobutyric acid ( Abu), is bound.Results: the overall structure of native CGL and complexed with alpha- methyl- mannoside and Abu have been refined at 2.3 angstrom and 2.31 angstrom resolution, respectively. Analysis of the electron density maps of the CGL structure shows clearly the presence of Abu, which was confirmed by mass spectrometry.Conclusion: the presence of Abu in a plant lectin structure strongly indicates the ability of lectins on carrying secondary metabolites. Comparison of the amino acids composing the site with other legume lectins revealed that this site is conserved, providing an evidence of the biological relevance of this site. This new action of lectins strengthens their role in defense mechanisms in plants.
publishDate 2007
dc.date.none.fl_str_mv 2007-08-02
2014-05-20T15:20:31Z
2014-05-20T15:20:31Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1186/1472-6807-7-52
Bmc Structural Biology. London: Biomed Central Ltd., v. 7, 9 p., 2007.
1471-2237
http://hdl.handle.net/11449/31796
10.1186/1472-6807-7-52
WOS:000249301900001
WOS000249301900001.pdf
url http://dx.doi.org/10.1186/1472-6807-7-52
http://hdl.handle.net/11449/31796
identifier_str_mv Bmc Structural Biology. London: Biomed Central Ltd., v. 7, 9 p., 2007.
1471-2237
10.1186/1472-6807-7-52
WOS:000249301900001
WOS000249301900001.pdf
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Bmc Structural Biology
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 9
application/pdf
dc.publisher.none.fl_str_mv Biomed Central Ltd.
publisher.none.fl_str_mv Biomed Central Ltd.
dc.source.none.fl_str_mv Web of Science
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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