Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode
- Autores
- Ibáñez, Marina; Rey Burusco, M. Florencia; Gabrielsen, Mads; Franchini, Gisela Raquel; Riboldi Tunnicliffe, Alan; Roe, Andrew J.; Griffiths, Kate; Cooper, Alan; Córsico, Betina; Kennedy, Malcolm W.; Smith, Brian O.
- Año de publicación
- 2019
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Intracellular lipid-binding proteins (iLBPs) of the fatty acid-binding protein (FABP) family of animals transport, mainly fatty acids or retinoids, are confined to the cytosol and have highly similar 3D structures. In contrast, nematodes possess fatty acid-binding proteins (nemFABPs) that are secreted into the perivitelline fluid surrounding their developing embryos. We report structures of As-p18, a nemFABP of the large intestinal roundworm Ascaris suum, with ligand bound, determined using X-ray crystallography and nuclear magnetic resonance spectroscopy. In common with other FABPs, As-p18 comprises a ten β-strand barrel capped by two short α-helices, with the carboxylate head group of oleate tethered in the interior of the protein. However, As-p18 exhibits two distinctive longer loops amongst β-strands not previously seen in a FABP. One of these is adjacent to the presumed ligand entry portal, so it may help to target the protein for efficient loading or unloading of ligand. The second, larger loop is at the opposite end of the molecule and has no equivalent in any iLBP structure yet determined. As-p18 preferentially binds a single 18-carbon fatty acid lig- and in its central cavity but in an orientation that differs from iLBPs. The unusual structural features of nemFABPs may relate to resourcing of developing embryos of nematodes.
Fil: Ibáñez, Marina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Rey Burusco, M. Florencia. Universidad Nacional de La Plata. Facultad de Ciencias Médicas; Argentina
Fil: Gabrielsen, Mads. University of Glasgow; Reino Unido
Fil: Franchini, Gisela Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Riboldi Tunnicliffe, Alan. Australian Synchrotron; Australia
Fil: Roe, Andrew J.. University of Glasgow; Reino Unido
Fil: Griffiths, Kate. University of Glasgow; Reino Unido
Fil: Cooper, Alan. University of Glasgow; Reino Unido
Fil: Córsico, Betina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Kennedy, Malcolm W.. University of Glasgow; Reino Unido
Fil: Smith, Brian O.. University of Glasgow; Reino Unido - Materia
-
Fatty acid binding protein
Ascaris suum
Asp-18
Parasitic helminths - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/144285
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Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematodeIbáñez, MarinaRey Burusco, M. FlorenciaGabrielsen, MadsFranchini, Gisela RaquelRiboldi Tunnicliffe, AlanRoe, Andrew J.Griffiths, KateCooper, AlanCórsico, BetinaKennedy, Malcolm W.Smith, Brian O.Fatty acid binding proteinAscaris suumAsp-18Parasitic helminthshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Intracellular lipid-binding proteins (iLBPs) of the fatty acid-binding protein (FABP) family of animals transport, mainly fatty acids or retinoids, are confined to the cytosol and have highly similar 3D structures. In contrast, nematodes possess fatty acid-binding proteins (nemFABPs) that are secreted into the perivitelline fluid surrounding their developing embryos. We report structures of As-p18, a nemFABP of the large intestinal roundworm Ascaris suum, with ligand bound, determined using X-ray crystallography and nuclear magnetic resonance spectroscopy. In common with other FABPs, As-p18 comprises a ten β-strand barrel capped by two short α-helices, with the carboxylate head group of oleate tethered in the interior of the protein. However, As-p18 exhibits two distinctive longer loops amongst β-strands not previously seen in a FABP. One of these is adjacent to the presumed ligand entry portal, so it may help to target the protein for efficient loading or unloading of ligand. The second, larger loop is at the opposite end of the molecule and has no equivalent in any iLBP structure yet determined. As-p18 preferentially binds a single 18-carbon fatty acid lig- and in its central cavity but in an orientation that differs from iLBPs. The unusual structural features of nemFABPs may relate to resourcing of developing embryos of nematodes.Fil: Ibáñez, Marina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; ArgentinaFil: Rey Burusco, M. Florencia. Universidad Nacional de La Plata. Facultad de Ciencias Médicas; ArgentinaFil: Gabrielsen, Mads. University of Glasgow; Reino UnidoFil: Franchini, Gisela Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; ArgentinaFil: Riboldi Tunnicliffe, Alan. Australian Synchrotron; AustraliaFil: Roe, Andrew J.. University of Glasgow; Reino UnidoFil: Griffiths, Kate. University of Glasgow; Reino UnidoFil: Cooper, Alan. University of Glasgow; Reino UnidoFil: Córsico, Betina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; ArgentinaFil: Kennedy, Malcolm W.. University of Glasgow; Reino UnidoFil: Smith, Brian O.. University of Glasgow; Reino UnidoPortland Press2019-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/144285Ibáñez, Marina; Rey Burusco, M. Florencia; Gabrielsen, Mads; Franchini, Gisela Raquel; Riboldi Tunnicliffe, Alan; et al.; Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode; Portland Press; Bioscience Reports; 39; 7; 7-2019; 1-160144-84631573-4935CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://bioscirep.org/lookup/doi/10.1042/BSR20191292info:eu-repo/semantics/altIdentifier/doi/10.1042/BSR20191292info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:17:40Zoai:ri.conicet.gov.ar:11336/144285instacron: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 10:17:41.27CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode |
title |
Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode |
spellingShingle |
Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode Ibáñez, Marina Fatty acid binding protein Ascaris suum Asp-18 Parasitic helminths |
title_short |
Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode |
title_full |
Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode |
title_fullStr |
Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode |
title_full_unstemmed |
Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode |
title_sort |
Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode |
dc.creator.none.fl_str_mv |
Ibáñez, Marina Rey Burusco, M. Florencia Gabrielsen, Mads Franchini, Gisela Raquel Riboldi Tunnicliffe, Alan Roe, Andrew J. Griffiths, Kate Cooper, Alan Córsico, Betina Kennedy, Malcolm W. Smith, Brian O. |
author |
Ibáñez, Marina |
author_facet |
Ibáñez, Marina Rey Burusco, M. Florencia Gabrielsen, Mads Franchini, Gisela Raquel Riboldi Tunnicliffe, Alan Roe, Andrew J. Griffiths, Kate Cooper, Alan Córsico, Betina Kennedy, Malcolm W. Smith, Brian O. |
author_role |
author |
author2 |
Rey Burusco, M. Florencia Gabrielsen, Mads Franchini, Gisela Raquel Riboldi Tunnicliffe, Alan Roe, Andrew J. Griffiths, Kate Cooper, Alan Córsico, Betina Kennedy, Malcolm W. Smith, Brian O. |
author2_role |
author author author author author author author author author author |
dc.subject.none.fl_str_mv |
Fatty acid binding protein Ascaris suum Asp-18 Parasitic helminths |
topic |
Fatty acid binding protein Ascaris suum Asp-18 Parasitic helminths |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Intracellular lipid-binding proteins (iLBPs) of the fatty acid-binding protein (FABP) family of animals transport, mainly fatty acids or retinoids, are confined to the cytosol and have highly similar 3D structures. In contrast, nematodes possess fatty acid-binding proteins (nemFABPs) that are secreted into the perivitelline fluid surrounding their developing embryos. We report structures of As-p18, a nemFABP of the large intestinal roundworm Ascaris suum, with ligand bound, determined using X-ray crystallography and nuclear magnetic resonance spectroscopy. In common with other FABPs, As-p18 comprises a ten β-strand barrel capped by two short α-helices, with the carboxylate head group of oleate tethered in the interior of the protein. However, As-p18 exhibits two distinctive longer loops amongst β-strands not previously seen in a FABP. One of these is adjacent to the presumed ligand entry portal, so it may help to target the protein for efficient loading or unloading of ligand. The second, larger loop is at the opposite end of the molecule and has no equivalent in any iLBP structure yet determined. As-p18 preferentially binds a single 18-carbon fatty acid lig- and in its central cavity but in an orientation that differs from iLBPs. The unusual structural features of nemFABPs may relate to resourcing of developing embryos of nematodes. Fil: Ibáñez, Marina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina Fil: Rey Burusco, M. Florencia. Universidad Nacional de La Plata. Facultad de Ciencias Médicas; Argentina Fil: Gabrielsen, Mads. University of Glasgow; Reino Unido Fil: Franchini, Gisela Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina Fil: Riboldi Tunnicliffe, Alan. Australian Synchrotron; Australia Fil: Roe, Andrew J.. University of Glasgow; Reino Unido Fil: Griffiths, Kate. University of Glasgow; Reino Unido Fil: Cooper, Alan. University of Glasgow; Reino Unido Fil: Córsico, Betina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina Fil: Kennedy, Malcolm W.. University of Glasgow; Reino Unido Fil: Smith, Brian O.. University of Glasgow; Reino Unido |
description |
Intracellular lipid-binding proteins (iLBPs) of the fatty acid-binding protein (FABP) family of animals transport, mainly fatty acids or retinoids, are confined to the cytosol and have highly similar 3D structures. In contrast, nematodes possess fatty acid-binding proteins (nemFABPs) that are secreted into the perivitelline fluid surrounding their developing embryos. We report structures of As-p18, a nemFABP of the large intestinal roundworm Ascaris suum, with ligand bound, determined using X-ray crystallography and nuclear magnetic resonance spectroscopy. In common with other FABPs, As-p18 comprises a ten β-strand barrel capped by two short α-helices, with the carboxylate head group of oleate tethered in the interior of the protein. However, As-p18 exhibits two distinctive longer loops amongst β-strands not previously seen in a FABP. One of these is adjacent to the presumed ligand entry portal, so it may help to target the protein for efficient loading or unloading of ligand. The second, larger loop is at the opposite end of the molecule and has no equivalent in any iLBP structure yet determined. As-p18 preferentially binds a single 18-carbon fatty acid lig- and in its central cavity but in an orientation that differs from iLBPs. The unusual structural features of nemFABPs may relate to resourcing of developing embryos of nematodes. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-07 |
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/11336/144285 Ibáñez, Marina; Rey Burusco, M. Florencia; Gabrielsen, Mads; Franchini, Gisela Raquel; Riboldi Tunnicliffe, Alan; et al.; Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode; Portland Press; Bioscience Reports; 39; 7; 7-2019; 1-16 0144-8463 1573-4935 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/144285 |
identifier_str_mv |
Ibáñez, Marina; Rey Burusco, M. Florencia; Gabrielsen, Mads; Franchini, Gisela Raquel; Riboldi Tunnicliffe, Alan; et al.; Structure and ligand binding of As-p18, an extracellular fatty acid binding protein from the eggs of a parasitic nematode; Portland Press; Bioscience Reports; 39; 7; 7-2019; 1-16 0144-8463 1573-4935 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://bioscirep.org/lookup/doi/10.1042/BSR20191292 info:eu-repo/semantics/altIdentifier/doi/10.1042/BSR20191292 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Portland Press |
publisher.none.fl_str_mv |
Portland Press |
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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1844614131689193472 |
score |
13.070432 |