Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins

Autores
Mechaly, Ariel Edgardo; Bellomio, Augusto; Gil Cartón, David; Morante, Koldo; Valle, Mikel; Gonzalez Mañas, Juan Manuel; Guérin, Diego M. A.
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Pore-forming toxins (PFTs) are proteins that are secreted as soluble molecules and are inserted into membranes to form oligomeric transmembrane pores. In this paper, we report the crystal structure of Fragaceatoxin C (FraC), a PFT isolated from the sea anemone Actinia fragacea, at 1.8 resolution. It consists of a crown-shaped nonamer with an external diameter of about 11.0 nm and an internal diameter of approximately 5.0 nm. Cryoelectron microscopy studies of FraC in lipid bilayers reveal the pore structure that traverses the membrane. The shape and dimensions of the crystallographic oligomer are fully consistent with the membrane pore. The FraC structure provides insight into the interactions governing the assembly process and suggests the structural changes that allow for membrane insertion. We propose a nonameric pore model that spans the membrane by forming a lipid-free α-helical bundle pore.
Fil: Mechaly, Ariel Edgardo. Universidad del País Vasco; España
Fil: Bellomio, Augusto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina. Universidad del País Vasco; España
Fil: Gil Cartón, David. Cooperative Center for Research in Biosciences; España
Fil: Morante, Koldo. Universidad del País Vasco; España
Fil: Valle, Mikel. Universidad del País Vasco; España
Fil: Gonzalez Mañas, Juan Manuel. Universidad del País Vasco; España
Fil: Guérin, Diego M. A.. Universidad del País Vasco; España
Materia
Membrane Pore
Toxins
Actinoporins
Pore-Forming Proteins
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:11336/62824
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxinsMechaly, Ariel EdgardoBellomio, AugustoGil Cartón, DavidMorante, KoldoValle, MikelGonzalez Mañas, Juan ManuelGuérin, Diego M. A.Membrane PoreToxinsActinoporinsPore-Forming Proteinshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Pore-forming toxins (PFTs) are proteins that are secreted as soluble molecules and are inserted into membranes to form oligomeric transmembrane pores. In this paper, we report the crystal structure of Fragaceatoxin C (FraC), a PFT isolated from the sea anemone Actinia fragacea, at 1.8 resolution. It consists of a crown-shaped nonamer with an external diameter of about 11.0 nm and an internal diameter of approximately 5.0 nm. Cryoelectron microscopy studies of FraC in lipid bilayers reveal the pore structure that traverses the membrane. The shape and dimensions of the crystallographic oligomer are fully consistent with the membrane pore. The FraC structure provides insight into the interactions governing the assembly process and suggests the structural changes that allow for membrane insertion. We propose a nonameric pore model that spans the membrane by forming a lipid-free α-helical bundle pore.Fil: Mechaly, Ariel Edgardo. Universidad del País Vasco; EspañaFil: Bellomio, Augusto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina. Universidad del País Vasco; EspañaFil: Gil Cartón, David. Cooperative Center for Research in Biosciences; EspañaFil: Morante, Koldo. Universidad del País Vasco; EspañaFil: Valle, Mikel. Universidad del País Vasco; EspañaFil: Gonzalez Mañas, Juan Manuel. Universidad del País Vasco; EspañaFil: Guérin, Diego M. A.. Universidad del País Vasco; EspañaElsevier2011-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/62824Mechaly, Ariel Edgardo; Bellomio, Augusto; Gil Cartón, David; Morante, Koldo; Valle, Mikel; et al.; Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins; Elsevier; Structure With Folding & Design.; 19; 2; 2-2011; 181-1910969-2126CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.str.2010.11.013info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0969212610004375info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:16:29Zoai:ri.conicet.gov.ar:11336/62824instacron: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:34982025-09-29 10:16:29.916CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins
title Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins
spellingShingle Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins
Mechaly, Ariel Edgardo
Membrane Pore
Toxins
Actinoporins
Pore-Forming Proteins
title_short Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins
title_full Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins
title_fullStr Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins
title_full_unstemmed Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins
title_sort Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins
dc.creator.none.fl_str_mv Mechaly, Ariel Edgardo
Bellomio, Augusto
Gil Cartón, David
Morante, Koldo
Valle, Mikel
Gonzalez Mañas, Juan Manuel
Guérin, Diego M. A.
author Mechaly, Ariel Edgardo
author_facet Mechaly, Ariel Edgardo
Bellomio, Augusto
Gil Cartón, David
Morante, Koldo
Valle, Mikel
Gonzalez Mañas, Juan Manuel
Guérin, Diego M. A.
author_role author
author2 Bellomio, Augusto
Gil Cartón, David
Morante, Koldo
Valle, Mikel
Gonzalez Mañas, Juan Manuel
Guérin, Diego M. A.
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Membrane Pore
Toxins
Actinoporins
Pore-Forming Proteins
topic Membrane Pore
Toxins
Actinoporins
Pore-Forming Proteins
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Pore-forming toxins (PFTs) are proteins that are secreted as soluble molecules and are inserted into membranes to form oligomeric transmembrane pores. In this paper, we report the crystal structure of Fragaceatoxin C (FraC), a PFT isolated from the sea anemone Actinia fragacea, at 1.8 resolution. It consists of a crown-shaped nonamer with an external diameter of about 11.0 nm and an internal diameter of approximately 5.0 nm. Cryoelectron microscopy studies of FraC in lipid bilayers reveal the pore structure that traverses the membrane. The shape and dimensions of the crystallographic oligomer are fully consistent with the membrane pore. The FraC structure provides insight into the interactions governing the assembly process and suggests the structural changes that allow for membrane insertion. We propose a nonameric pore model that spans the membrane by forming a lipid-free α-helical bundle pore.
Fil: Mechaly, Ariel Edgardo. Universidad del País Vasco; España
Fil: Bellomio, Augusto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina. Universidad del País Vasco; España
Fil: Gil Cartón, David. Cooperative Center for Research in Biosciences; España
Fil: Morante, Koldo. Universidad del País Vasco; España
Fil: Valle, Mikel. Universidad del País Vasco; España
Fil: Gonzalez Mañas, Juan Manuel. Universidad del País Vasco; España
Fil: Guérin, Diego M. A.. Universidad del País Vasco; España
description Pore-forming toxins (PFTs) are proteins that are secreted as soluble molecules and are inserted into membranes to form oligomeric transmembrane pores. In this paper, we report the crystal structure of Fragaceatoxin C (FraC), a PFT isolated from the sea anemone Actinia fragacea, at 1.8 resolution. It consists of a crown-shaped nonamer with an external diameter of about 11.0 nm and an internal diameter of approximately 5.0 nm. Cryoelectron microscopy studies of FraC in lipid bilayers reveal the pore structure that traverses the membrane. The shape and dimensions of the crystallographic oligomer are fully consistent with the membrane pore. The FraC structure provides insight into the interactions governing the assembly process and suggests the structural changes that allow for membrane insertion. We propose a nonameric pore model that spans the membrane by forming a lipid-free α-helical bundle pore.
publishDate 2011
dc.date.none.fl_str_mv 2011-02
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/11336/62824
Mechaly, Ariel Edgardo; Bellomio, Augusto; Gil Cartón, David; Morante, Koldo; Valle, Mikel; et al.; Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins; Elsevier; Structure With Folding & Design.; 19; 2; 2-2011; 181-191
0969-2126
CONICET Digital
CONICET
url http://hdl.handle.net/11336/62824
identifier_str_mv Mechaly, Ariel Edgardo; Bellomio, Augusto; Gil Cartón, David; Morante, Koldo; Valle, Mikel; et al.; Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins; Elsevier; Structure With Folding & Design.; 19; 2; 2-2011; 181-191
0969-2126
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.str.2010.11.013
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0969212610004375
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
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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 13.070432

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