Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20

Autores
Otrelo Cardoso, Ana Rita; Nair, Rashmi R.; Correia, Márcia A. S.; Correia Cordeiro, RAquel S.; Panjkovich, Alejandro; Svergun, Dmitri I.; Santos Silva, Teresa; Rivas, Maria Gabriela
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Molybdenum and tungsten are taken up by bacteria and archaea as their soluble oxyanions through high affinity transport systems belonging to the ATP-binding cassette (ABC) transporters. The component A (ModA/TupA) of these transporters is the first selection gate from which the cell differentiates between MoO4 2-, WO4 2- and other similar oxyanions. We report the biochemical characterization and the crystal structure of the apo-TupA from Desulfovibrio desulfuricans G20, at 1.4 Å resolution. Small Angle X-ray Scattering data suggests that the protein adopts a closed and more stable conformation upon ion binding. The role of the arginine 118 in the selectivity of the oxyanion was also investigated and three mutants were constructed: R118K, R118E and R118Q. Isothermal titration calorimetry clearly shows the relevance of this residue for metal discrimination and oxyanion binding. In this sense, the three variants lost the ability to coordinate molybdate and the R118K mutant keeps an extremely high affinity for tungstate. These results contribute to an understanding of the metal-protein interaction, making it a suitable candidate for a recognition element of a biosensor for tungsten detection.
Fil: Otrelo Cardoso, Ana Rita. Universidade Nova de Lisboa; Portugal
Fil: Nair, Rashmi R.. Universidade Nova de Lisboa; Portugal
Fil: Correia, Márcia A. S.. Universidade Nova de Lisboa; Portugal
Fil: Correia Cordeiro, RAquel S.. Universidade Nova de Lisboa; Portugal
Fil: Panjkovich, Alejandro. European Molecular Biology Laboratory; Alemania
Fil: Svergun, Dmitri I.. European Molecular Biology Laboratory; Alemania
Fil: Santos Silva, Teresa. Universidade Nova de Lisboa; Portugal
Fil: Rivas, Maria Gabriela. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina
Materia
TUNGSTEN
MOLYBDENUM
METAL TRANSPORT
SULFATE REDUCING BACTERIA
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:11336/85356

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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20Otrelo Cardoso, Ana RitaNair, Rashmi R.Correia, Márcia A. S.Correia Cordeiro, RAquel S.Panjkovich, AlejandroSvergun, Dmitri I.Santos Silva, TeresaRivas, Maria GabrielaTUNGSTENMOLYBDENUMMETAL TRANSPORTSULFATE REDUCING BACTERIAhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Molybdenum and tungsten are taken up by bacteria and archaea as their soluble oxyanions through high affinity transport systems belonging to the ATP-binding cassette (ABC) transporters. The component A (ModA/TupA) of these transporters is the first selection gate from which the cell differentiates between MoO4 2-, WO4 2- and other similar oxyanions. We report the biochemical characterization and the crystal structure of the apo-TupA from Desulfovibrio desulfuricans G20, at 1.4 Å resolution. Small Angle X-ray Scattering data suggests that the protein adopts a closed and more stable conformation upon ion binding. The role of the arginine 118 in the selectivity of the oxyanion was also investigated and three mutants were constructed: R118K, R118E and R118Q. Isothermal titration calorimetry clearly shows the relevance of this residue for metal discrimination and oxyanion binding. In this sense, the three variants lost the ability to coordinate molybdate and the R118K mutant keeps an extremely high affinity for tungstate. These results contribute to an understanding of the metal-protein interaction, making it a suitable candidate for a recognition element of a biosensor for tungsten detection.Fil: Otrelo Cardoso, Ana Rita. Universidade Nova de Lisboa; PortugalFil: Nair, Rashmi R.. Universidade Nova de Lisboa; PortugalFil: Correia, Márcia A. S.. Universidade Nova de Lisboa; PortugalFil: Correia Cordeiro, RAquel S.. Universidade Nova de Lisboa; PortugalFil: Panjkovich, Alejandro. European Molecular Biology Laboratory; AlemaniaFil: Svergun, Dmitri I.. European Molecular Biology Laboratory; AlemaniaFil: Santos Silva, Teresa. Universidade Nova de Lisboa; PortugalFil: Rivas, Maria Gabriela. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; ArgentinaNature Publishing Group2017-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/85356Otrelo Cardoso, Ana Rita; Nair, Rashmi R.; Correia, Márcia A. S.; Correia Cordeiro, RAquel S.; Panjkovich, Alejandro; et al.; Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20; Nature Publishing Group; Scientific Reports; 7; 12-2017; 1-12; 57982045-2322CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-017-06133-yinfo:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/s41598-017-06133-yinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:00:50Zoai:ri.conicet.gov.ar:11336/85356instacron: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:34982025-09-03 10:00:50.92CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20
title Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20
spellingShingle Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20
Otrelo Cardoso, Ana Rita
TUNGSTEN
MOLYBDENUM
METAL TRANSPORT
SULFATE REDUCING BACTERIA
title_short Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20
title_full Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20
title_fullStr Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20
title_full_unstemmed Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20
title_sort Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20
dc.creator.none.fl_str_mv Otrelo Cardoso, Ana Rita
Nair, Rashmi R.
Correia, Márcia A. S.
Correia Cordeiro, RAquel S.
Panjkovich, Alejandro
Svergun, Dmitri I.
Santos Silva, Teresa
Rivas, Maria Gabriela
author Otrelo Cardoso, Ana Rita
author_facet Otrelo Cardoso, Ana Rita
Nair, Rashmi R.
Correia, Márcia A. S.
Correia Cordeiro, RAquel S.
Panjkovich, Alejandro
Svergun, Dmitri I.
Santos Silva, Teresa
Rivas, Maria Gabriela
author_role author
author2 Nair, Rashmi R.
Correia, Márcia A. S.
Correia Cordeiro, RAquel S.
Panjkovich, Alejandro
Svergun, Dmitri I.
Santos Silva, Teresa
Rivas, Maria Gabriela
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv TUNGSTEN
MOLYBDENUM
METAL TRANSPORT
SULFATE REDUCING BACTERIA
topic TUNGSTEN
MOLYBDENUM
METAL TRANSPORT
SULFATE REDUCING BACTERIA
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Molybdenum and tungsten are taken up by bacteria and archaea as their soluble oxyanions through high affinity transport systems belonging to the ATP-binding cassette (ABC) transporters. The component A (ModA/TupA) of these transporters is the first selection gate from which the cell differentiates between MoO4 2-, WO4 2- and other similar oxyanions. We report the biochemical characterization and the crystal structure of the apo-TupA from Desulfovibrio desulfuricans G20, at 1.4 Å resolution. Small Angle X-ray Scattering data suggests that the protein adopts a closed and more stable conformation upon ion binding. The role of the arginine 118 in the selectivity of the oxyanion was also investigated and three mutants were constructed: R118K, R118E and R118Q. Isothermal titration calorimetry clearly shows the relevance of this residue for metal discrimination and oxyanion binding. In this sense, the three variants lost the ability to coordinate molybdate and the R118K mutant keeps an extremely high affinity for tungstate. These results contribute to an understanding of the metal-protein interaction, making it a suitable candidate for a recognition element of a biosensor for tungsten detection.
Fil: Otrelo Cardoso, Ana Rita. Universidade Nova de Lisboa; Portugal
Fil: Nair, Rashmi R.. Universidade Nova de Lisboa; Portugal
Fil: Correia, Márcia A. S.. Universidade Nova de Lisboa; Portugal
Fil: Correia Cordeiro, RAquel S.. Universidade Nova de Lisboa; Portugal
Fil: Panjkovich, Alejandro. European Molecular Biology Laboratory; Alemania
Fil: Svergun, Dmitri I.. European Molecular Biology Laboratory; Alemania
Fil: Santos Silva, Teresa. Universidade Nova de Lisboa; Portugal
Fil: Rivas, Maria Gabriela. Universidad Nacional del Litoral. Facultad de Bioquímica y Ciencias Biológicas. Departamento de Física; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe; Argentina
description Molybdenum and tungsten are taken up by bacteria and archaea as their soluble oxyanions through high affinity transport systems belonging to the ATP-binding cassette (ABC) transporters. The component A (ModA/TupA) of these transporters is the first selection gate from which the cell differentiates between MoO4 2-, WO4 2- and other similar oxyanions. We report the biochemical characterization and the crystal structure of the apo-TupA from Desulfovibrio desulfuricans G20, at 1.4 Å resolution. Small Angle X-ray Scattering data suggests that the protein adopts a closed and more stable conformation upon ion binding. The role of the arginine 118 in the selectivity of the oxyanion was also investigated and three mutants were constructed: R118K, R118E and R118Q. Isothermal titration calorimetry clearly shows the relevance of this residue for metal discrimination and oxyanion binding. In this sense, the three variants lost the ability to coordinate molybdate and the R118K mutant keeps an extremely high affinity for tungstate. These results contribute to an understanding of the metal-protein interaction, making it a suitable candidate for a recognition element of a biosensor for tungsten detection.
publishDate 2017
dc.date.none.fl_str_mv 2017-12
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/11336/85356
Otrelo Cardoso, Ana Rita; Nair, Rashmi R.; Correia, Márcia A. S.; Correia Cordeiro, RAquel S.; Panjkovich, Alejandro; et al.; Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20; Nature Publishing Group; Scientific Reports; 7; 12-2017; 1-12; 5798
2045-2322
CONICET Digital
CONICET
url http://hdl.handle.net/11336/85356
identifier_str_mv Otrelo Cardoso, Ana Rita; Nair, Rashmi R.; Correia, Márcia A. S.; Correia Cordeiro, RAquel S.; Panjkovich, Alejandro; et al.; Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20; Nature Publishing Group; Scientific Reports; 7; 12-2017; 1-12; 5798
2045-2322
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-017-06133-y
info:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/s41598-017-06133-y
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 Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
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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