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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/85356
Ver los metadatos del registro completo
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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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1842269662486724608 |
score |
13.13397 |