High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP-oleic acid complex: Study of the internal water cluster and ligand binding by a transferred mult...

Autores
Howard, Eduardo Ignacio; Guillot, B.; Blakeley, M. P.; Haertlein, M.; Moulin, M.; Mitschler, A.; Cousido Siah, A.; Fadel, F.; Valsecchi, Wanda Mariela; Tomizaki, Takashi; Petrova, T.; Claudot, J.; Podjarny, Alberto Daniel
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Crystal diffraction data of heart fatty acid binding protein (H-FABP) in complex with oleic acid were measured at room temperature with high-resolution X-ray and neutron protein crystallography (0.98 and 1.90 Å resolution, respectively). These data provided very detailed information about the cluster of water molecules and the bound oleic acid in the H-FABP large internal cavity. The jointly refined X-ray/neutron structure of H-FABP was complemented by a transferred multipolar electron-density distribution using the parameters of the ELMAMII library. The resulting electron density allowed a precise determination of the electrostatic potential in the fatty acid (FA) binding pocket. Bader's quantum theory of atoms in molecules was then used to study interactions involving the internal water molecules, the FA and the protein. This approach showed H···H contacts of the FA with highly conserved hydrophobic residues known to play a role in the stabilization of long-chain FAs in the binding cavity. The determination of water hydrogen (deuterium) positions allowed the analysis of the orientation and electrostatic properties of the water molecules in the very ordered cluster. As a result, a significant alignment of the permanent dipoles of the water molecules with the protein electrostatic field was observed. This can be related to the dielectric properties of hydration layers around proteins, where the shielding of electrostatic interactions depends directly on the rotational degrees of freedom of the water molecules in the interface.
Fil: Howard, Eduardo Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina. Centre National de la Recherche Scientifique. Igbmc; Francia. Inserm; Francia
Fil: Guillot, B.. Centre National de la Recherche Scientifique; Francia
Fil: Blakeley, M. P.. Institut Laue Langevin; Francia
Fil: Haertlein, M.. Institut Laue Langevin; Francia
Fil: Moulin, M.. Institut Laue Langevin; Francia
Fil: Mitschler, A.. Centre National de la Recherche Scientifique. Igbmc; Francia. Inserm; Francia
Fil: Cousido Siah, A.. Centre National de la Recherche Scientifique. Igbmc; Francia. Inserm; Francia
Fil: Fadel, F.. Centre National de la Recherche Scientifique. Igbmc; Francia. Inserm; Francia
Fil: Valsecchi, Wanda Mariela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-química Biológicas "prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-química Biológicas; Argentina
Fil: Tomizaki, Takashi. Paul Scherrer Institute; Suiza
Fil: Petrova, T.. Russian Academy of Sciences. Institute of Mathematical Problems of Biology ; Rusia
Fil: Claudot, J.. Centre National de la Recherche Scientifique; Francia
Fil: Podjarny, Alberto Daniel. Centre National de la Recherche Scientifique. Igbmc; Francia. Inserm; Francia
Materia
AIM TOPOLOGICAL PROPERTIES
FATTY ACID BINDING PROTEIN
HIGH-RESOLUTION ROOM-TEMPERATURE X-RAY CRYSTALLOGRAPHY
NEUTRON PROTEIN CRYSTALLOGRAPHY
PROTEIN HYDRATION LAYER
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:11336/18498
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/18498
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP-oleic acid complex: Study of the internal water cluster and ligand binding by a transferred multipolar electron-density distributionHoward, Eduardo IgnacioGuillot, B.Blakeley, M. P.Haertlein, M.Moulin, M.Mitschler, A.Cousido Siah, A.Fadel, F.Valsecchi, Wanda MarielaTomizaki, TakashiPetrova, T.Claudot, J.Podjarny, Alberto DanielAIM TOPOLOGICAL PROPERTIESFATTY ACID BINDING PROTEINHIGH-RESOLUTION ROOM-TEMPERATURE X-RAY CRYSTALLOGRAPHYNEUTRON PROTEIN CRYSTALLOGRAPHYPROTEIN HYDRATION LAYERhttps://purl.org/becyt/ford/1.7https://purl.org/becyt/ford/1Crystal diffraction data of heart fatty acid binding protein (H-FABP) in complex with oleic acid were measured at room temperature with high-resolution X-ray and neutron protein crystallography (0.98 and 1.90 Å resolution, respectively). These data provided very detailed information about the cluster of water molecules and the bound oleic acid in the H-FABP large internal cavity. The jointly refined X-ray/neutron structure of H-FABP was complemented by a transferred multipolar electron-density distribution using the parameters of the ELMAMII library. The resulting electron density allowed a precise determination of the electrostatic potential in the fatty acid (FA) binding pocket. Bader's quantum theory of atoms in molecules was then used to study interactions involving the internal water molecules, the FA and the protein. This approach showed H···H contacts of the FA with highly conserved hydrophobic residues known to play a role in the stabilization of long-chain FAs in the binding cavity. The determination of water hydrogen (deuterium) positions allowed the analysis of the orientation and electrostatic properties of the water molecules in the very ordered cluster. As a result, a significant alignment of the permanent dipoles of the water molecules with the protein electrostatic field was observed. This can be related to the dielectric properties of hydration layers around proteins, where the shielding of electrostatic interactions depends directly on the rotational degrees of freedom of the water molecules in the interface.Fil: Howard, Eduardo Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina. Centre National de la Recherche Scientifique. Igbmc; Francia. Inserm; FranciaFil: Guillot, B.. Centre National de la Recherche Scientifique; FranciaFil: Blakeley, M. P.. Institut Laue Langevin; FranciaFil: Haertlein, M.. Institut Laue Langevin; FranciaFil: Moulin, M.. Institut Laue Langevin; FranciaFil: Mitschler, A.. Centre National de la Recherche Scientifique. Igbmc; Francia. Inserm; FranciaFil: Cousido Siah, A.. Centre National de la Recherche Scientifique. Igbmc; Francia. Inserm; FranciaFil: Fadel, F.. Centre National de la Recherche Scientifique. Igbmc; Francia. Inserm; FranciaFil: Valsecchi, Wanda Mariela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-química Biológicas "prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-química Biológicas; ArgentinaFil: Tomizaki, Takashi. Paul Scherrer Institute; SuizaFil: Petrova, T.. Russian Academy of Sciences. Institute of Mathematical Problems of Biology ; RusiaFil: Claudot, J.. Centre National de la Recherche Scientifique; FranciaFil: Podjarny, Alberto Daniel. Centre National de la Recherche Scientifique. Igbmc; Francia. Inserm; FranciaInternational Union of Crystallography2016-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/18498Howard, Eduardo Ignacio; Guillot, B.; Blakeley, M. P.; Haertlein, M.; Moulin, M.; et al.; High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP-oleic acid complex: Study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution; International Union of Crystallography; IUCrJ; 3; part 2; 3-2016; 115-1262052-2525CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://journals.iucr.org/m/issues/2016/02/00/tj5008/index.htmlinfo:eu-repo/semantics/altIdentifier/doi/10.1107/S2052252515024161info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4775160/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:34:07Zoai:ri.conicet.gov.ar:11336/18498instacron: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 10:34:08.143CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP-oleic acid complex: Study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution
title High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP-oleic acid complex: Study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution
spellingShingle High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP-oleic acid complex: Study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution
Howard, Eduardo Ignacio
AIM TOPOLOGICAL PROPERTIES
FATTY ACID BINDING PROTEIN
HIGH-RESOLUTION ROOM-TEMPERATURE X-RAY CRYSTALLOGRAPHY
NEUTRON PROTEIN CRYSTALLOGRAPHY
PROTEIN HYDRATION LAYER
title_short High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP-oleic acid complex: Study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution
title_full High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP-oleic acid complex: Study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution
title_fullStr High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP-oleic acid complex: Study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution
title_full_unstemmed High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP-oleic acid complex: Study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution
title_sort High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP-oleic acid complex: Study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution
dc.creator.none.fl_str_mv Howard, Eduardo Ignacio
Guillot, B.
Blakeley, M. P.
Haertlein, M.
Moulin, M.
Mitschler, A.
Cousido Siah, A.
Fadel, F.
Valsecchi, Wanda Mariela
Tomizaki, Takashi
Petrova, T.
Claudot, J.
Podjarny, Alberto Daniel
author Howard, Eduardo Ignacio
author_facet Howard, Eduardo Ignacio
Guillot, B.
Blakeley, M. P.
Haertlein, M.
Moulin, M.
Mitschler, A.
Cousido Siah, A.
Fadel, F.
Valsecchi, Wanda Mariela
Tomizaki, Takashi
Petrova, T.
Claudot, J.
Podjarny, Alberto Daniel
author_role author
author2 Guillot, B.
Blakeley, M. P.
Haertlein, M.
Moulin, M.
Mitschler, A.
Cousido Siah, A.
Fadel, F.
Valsecchi, Wanda Mariela
Tomizaki, Takashi
Petrova, T.
Claudot, J.
Podjarny, Alberto Daniel
author2_role author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv AIM TOPOLOGICAL PROPERTIES
FATTY ACID BINDING PROTEIN
HIGH-RESOLUTION ROOM-TEMPERATURE X-RAY CRYSTALLOGRAPHY
NEUTRON PROTEIN CRYSTALLOGRAPHY
PROTEIN HYDRATION LAYER
topic AIM TOPOLOGICAL PROPERTIES
FATTY ACID BINDING PROTEIN
HIGH-RESOLUTION ROOM-TEMPERATURE X-RAY CRYSTALLOGRAPHY
NEUTRON PROTEIN CRYSTALLOGRAPHY
PROTEIN HYDRATION LAYER
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.7
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Crystal diffraction data of heart fatty acid binding protein (H-FABP) in complex with oleic acid were measured at room temperature with high-resolution X-ray and neutron protein crystallography (0.98 and 1.90 Å resolution, respectively). These data provided very detailed information about the cluster of water molecules and the bound oleic acid in the H-FABP large internal cavity. The jointly refined X-ray/neutron structure of H-FABP was complemented by a transferred multipolar electron-density distribution using the parameters of the ELMAMII library. The resulting electron density allowed a precise determination of the electrostatic potential in the fatty acid (FA) binding pocket. Bader's quantum theory of atoms in molecules was then used to study interactions involving the internal water molecules, the FA and the protein. This approach showed H···H contacts of the FA with highly conserved hydrophobic residues known to play a role in the stabilization of long-chain FAs in the binding cavity. The determination of water hydrogen (deuterium) positions allowed the analysis of the orientation and electrostatic properties of the water molecules in the very ordered cluster. As a result, a significant alignment of the permanent dipoles of the water molecules with the protein electrostatic field was observed. This can be related to the dielectric properties of hydration layers around proteins, where the shielding of electrostatic interactions depends directly on the rotational degrees of freedom of the water molecules in the interface.
Fil: Howard, Eduardo Ignacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Física de Líquidos y Sistemas Biológicos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Física de Líquidos y Sistemas Biológicos; Argentina. Centre National de la Recherche Scientifique. Igbmc; Francia. Inserm; Francia
Fil: Guillot, B.. Centre National de la Recherche Scientifique; Francia
Fil: Blakeley, M. P.. Institut Laue Langevin; Francia
Fil: Haertlein, M.. Institut Laue Langevin; Francia
Fil: Moulin, M.. Institut Laue Langevin; Francia
Fil: Mitschler, A.. Centre National de la Recherche Scientifique. Igbmc; Francia. Inserm; Francia
Fil: Cousido Siah, A.. Centre National de la Recherche Scientifique. Igbmc; Francia. Inserm; Francia
Fil: Fadel, F.. Centre National de la Recherche Scientifique. Igbmc; Francia. Inserm; Francia
Fil: Valsecchi, Wanda Mariela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-química Biológicas "prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-química Biológicas; Argentina
Fil: Tomizaki, Takashi. Paul Scherrer Institute; Suiza
Fil: Petrova, T.. Russian Academy of Sciences. Institute of Mathematical Problems of Biology ; Rusia
Fil: Claudot, J.. Centre National de la Recherche Scientifique; Francia
Fil: Podjarny, Alberto Daniel. Centre National de la Recherche Scientifique. Igbmc; Francia. Inserm; Francia
description Crystal diffraction data of heart fatty acid binding protein (H-FABP) in complex with oleic acid were measured at room temperature with high-resolution X-ray and neutron protein crystallography (0.98 and 1.90 Å resolution, respectively). These data provided very detailed information about the cluster of water molecules and the bound oleic acid in the H-FABP large internal cavity. The jointly refined X-ray/neutron structure of H-FABP was complemented by a transferred multipolar electron-density distribution using the parameters of the ELMAMII library. The resulting electron density allowed a precise determination of the electrostatic potential in the fatty acid (FA) binding pocket. Bader's quantum theory of atoms in molecules was then used to study interactions involving the internal water molecules, the FA and the protein. This approach showed H···H contacts of the FA with highly conserved hydrophobic residues known to play a role in the stabilization of long-chain FAs in the binding cavity. The determination of water hydrogen (deuterium) positions allowed the analysis of the orientation and electrostatic properties of the water molecules in the very ordered cluster. As a result, a significant alignment of the permanent dipoles of the water molecules with the protein electrostatic field was observed. This can be related to the dielectric properties of hydration layers around proteins, where the shielding of electrostatic interactions depends directly on the rotational degrees of freedom of the water molecules in the interface.
publishDate 2016
dc.date.none.fl_str_mv 2016-03
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/11336/18498
Howard, Eduardo Ignacio; Guillot, B.; Blakeley, M. P.; Haertlein, M.; Moulin, M.; et al.; High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP-oleic acid complex: Study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution; International Union of Crystallography; IUCrJ; 3; part 2; 3-2016; 115-126
2052-2525
CONICET Digital
CONICET
url http://hdl.handle.net/11336/18498
identifier_str_mv Howard, Eduardo Ignacio; Guillot, B.; Blakeley, M. P.; Haertlein, M.; Moulin, M.; et al.; High-resolution neutron and X-ray diffraction room-temperature studies of an H-FABP-oleic acid complex: Study of the internal water cluster and ligand binding by a transferred multipolar electron-density distribution; International Union of Crystallography; IUCrJ; 3; part 2; 3-2016; 115-126
2052-2525
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://journals.iucr.org/m/issues/2016/02/00/tj5008/index.html
info:eu-repo/semantics/altIdentifier/doi/10.1107/S2052252515024161
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4775160/
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 International Union of Crystallography
publisher.none.fl_str_mv International Union of Crystallography
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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