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 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

SUBMITTER: Otrelo-Cardoso AR 

PROVIDER: S-EPMC5517513 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature