Structure of ß-cinnamomin, a protein toxic to some plant species
Autor(a) principal: | |
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Data de Publicação: | 2002 |
Outros Autores: | , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.1/1218 |
Resumo: | Phytophthora and Pythium species are among the most aggressive plant pathogens, as they invade many economically important crops and forest trees. They secrete large amounts of 10 kDa proteins called elicitins that can act as elicitors of plant defence mechanisms. These proteins may also induce a hypersensitive response (HR) including plant cell necrosis, with different levels of toxicity depending on their pI. Recent studies showed that elicitins function as sterol carrier proteins. The crystallographic structure of the highly necrotic recombinant -cinnamomin ( -CIN) from Phytophthora cinnamomi has been determined at 1.8 A Ê resolution using the molecularreplacement method. -CIN has the same overall structure as -cryptogein ( -CRY), an elicitin secreted by Phytophthora cryptogea, although it shows a different surface electrostatic potential distribution. The protein was expressed in Pichia pastoris and crystallized in the triclinic space group with two monomers in the asymmetric unit. The interface formed by these two monomers resembles that from -CRY dimer, although with fewer interactions. |
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Structure of ß-cinnamomin, a protein toxic to some plant speciesBeta-cinnamominElicitinsPhytophthora and Pythium species are among the most aggressive plant pathogens, as they invade many economically important crops and forest trees. They secrete large amounts of 10 kDa proteins called elicitins that can act as elicitors of plant defence mechanisms. These proteins may also induce a hypersensitive response (HR) including plant cell necrosis, with different levels of toxicity depending on their pI. Recent studies showed that elicitins function as sterol carrier proteins. The crystallographic structure of the highly necrotic recombinant -cinnamomin ( -CIN) from Phytophthora cinnamomi has been determined at 1.8 A Ê resolution using the molecularreplacement method. -CIN has the same overall structure as -cryptogein ( -CRY), an elicitin secreted by Phytophthora cryptogea, although it shows a different surface electrostatic potential distribution. The protein was expressed in Pichia pastoris and crystallized in the triclinic space group with two monomers in the asymmetric unit. The interface formed by these two monomers resembles that from -CRY dimer, although with fewer interactions.SapientiaRodrigues, Maria LuisaArcher, MargaridaMartel, PauloJacquet, AlainCravador, A.Carrondo, Maria A.2012-06-09T10:50:55Z20022012-05-24T20:25:37Z2002-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.1/1218engRodrigues, Maria L.; Archer, Margarida; Martel, Paulo; Jacquet, Alain; Cravador, Alfredo; Carrondo, Maria A. Structure of ß-cinnamomin, a protein toxic to some plant species. Acta Crystallographica. Section D. Biological Crystallography, 58, 8, 1314-1321, 2002.09074449AUT: ACR00659; PMA01479;info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-24T10:12:17Zoai:sapientia.ualg.pt:10400.1/1218Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:55:27.346009Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Structure of ß-cinnamomin, a protein toxic to some plant species |
title |
Structure of ß-cinnamomin, a protein toxic to some plant species |
spellingShingle |
Structure of ß-cinnamomin, a protein toxic to some plant species Rodrigues, Maria Luisa Beta-cinnamomin Elicitins |
title_short |
Structure of ß-cinnamomin, a protein toxic to some plant species |
title_full |
Structure of ß-cinnamomin, a protein toxic to some plant species |
title_fullStr |
Structure of ß-cinnamomin, a protein toxic to some plant species |
title_full_unstemmed |
Structure of ß-cinnamomin, a protein toxic to some plant species |
title_sort |
Structure of ß-cinnamomin, a protein toxic to some plant species |
author |
Rodrigues, Maria Luisa |
author_facet |
Rodrigues, Maria Luisa Archer, Margarida Martel, Paulo Jacquet, Alain Cravador, A. Carrondo, Maria A. |
author_role |
author |
author2 |
Archer, Margarida Martel, Paulo Jacquet, Alain Cravador, A. Carrondo, Maria A. |
author2_role |
author author author author author |
dc.contributor.none.fl_str_mv |
Sapientia |
dc.contributor.author.fl_str_mv |
Rodrigues, Maria Luisa Archer, Margarida Martel, Paulo Jacquet, Alain Cravador, A. Carrondo, Maria A. |
dc.subject.por.fl_str_mv |
Beta-cinnamomin Elicitins |
topic |
Beta-cinnamomin Elicitins |
description |
Phytophthora and Pythium species are among the most aggressive plant pathogens, as they invade many economically important crops and forest trees. They secrete large amounts of 10 kDa proteins called elicitins that can act as elicitors of plant defence mechanisms. These proteins may also induce a hypersensitive response (HR) including plant cell necrosis, with different levels of toxicity depending on their pI. Recent studies showed that elicitins function as sterol carrier proteins. The crystallographic structure of the highly necrotic recombinant -cinnamomin ( -CIN) from Phytophthora cinnamomi has been determined at 1.8 A Ê resolution using the molecularreplacement method. -CIN has the same overall structure as -cryptogein ( -CRY), an elicitin secreted by Phytophthora cryptogea, although it shows a different surface electrostatic potential distribution. The protein was expressed in Pichia pastoris and crystallized in the triclinic space group with two monomers in the asymmetric unit. The interface formed by these two monomers resembles that from -CRY dimer, although with fewer interactions. |
publishDate |
2002 |
dc.date.none.fl_str_mv |
2002 2002-01-01T00:00:00Z 2012-06-09T10:50:55Z 2012-05-24T20:25:37Z |
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://hdl.handle.net/10400.1/1218 |
url |
http://hdl.handle.net/10400.1/1218 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Rodrigues, Maria L.; Archer, Margarida; Martel, Paulo; Jacquet, Alain; Cravador, Alfredo; Carrondo, Maria A. Structure of ß-cinnamomin, a protein toxic to some plant species. Acta Crystallographica. Section D. Biological Crystallography, 58, 8, 1314-1321, 2002. 09074449 AUT: ACR00659; PMA01479; |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
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RCAAP |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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1799133157109268480 |