Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20

Abstract 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 differe...

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Autores principales:	Ana Rita Otrelo-Cardoso, Rashmi R. Nair, Márcia A. S. Correia, Raquel S. Correia Cordeiro, Alejandro Panjkovich, Dmitri I. Svergun, Teresa Santos-Silva, Maria G. Rivas
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ad4b6ab3f0d04375a038f7e830372ad1
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spelling	oai:doaj.org-article:ad4b6ab3f0d04375a038f7e830372ad12021-12-02T15:06:11ZHighly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G2010.1038/s41598-017-06133-y2045-2322https://doaj.org/article/ad4b6ab3f0d04375a038f7e830372ad12017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-06133-yhttps://doaj.org/toc/2045-2322Abstract 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.Ana Rita Otrelo-CardosoRashmi R. NairMárcia A. S. CorreiaRaquel S. Correia CordeiroAlejandro PanjkovichDmitri I. SvergunTeresa Santos-SilvaMaria G. RivasNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ana Rita Otrelo-Cardoso Rashmi R. Nair Márcia A. S. Correia Raquel S. Correia Cordeiro Alejandro Panjkovich Dmitri I. Svergun Teresa Santos-Silva Maria G. Rivas Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20
description	Abstract 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.
format	article
author	Ana Rita Otrelo-Cardoso Rashmi R. Nair Márcia A. S. Correia Raquel S. Correia Cordeiro Alejandro Panjkovich Dmitri I. Svergun Teresa Santos-Silva Maria G. Rivas
author_facet	Ana Rita Otrelo-Cardoso Rashmi R. Nair Márcia A. S. Correia Raquel S. Correia Cordeiro Alejandro Panjkovich Dmitri I. Svergun Teresa Santos-Silva Maria G. Rivas
author_sort	Ana Rita Otrelo-Cardoso
title	Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20
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
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/ad4b6ab3f0d04375a038f7e830372ad1
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_version_	1718388603690680320

Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20

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