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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/144285
Acceder
id CONICETDig_d4c8c7c0bfd1eab1b0dd61fb1f842bf0
oai_identifier_str oai:ri.conicet.gov.ar:11336/144285
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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 Técnicas2025-10-22T11:47:59Zoai: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:34982025-10-22 11:47:59.308CONICET 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
_version_ 1846782185042870272
score 12.982451

Publicaciones similares