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5MY5

Tungstate binding protein - TupA - from Desulfovibrio alaskensis G20

5MY5 の概要
エントリーDOI10.2210/pdb5my5/pdb
分子名称ABC transporter periplasmic substrate-binding protein, SODIUM ION, CHLORIDE ION, ... (4 entities in total)
機能のキーワードsusbtrate binding protein, tupa, tungstate, desulfovibrio alaskensis g20, abc transporter, tungsten detection, sulphate reducing bacteria, transport protein
由来する生物種Desulfovibrio alaskensis (strain G20)
タンパク質・核酸の鎖数1
化学式量合計29791.78
構造登録者
Otrelo-Cardoso, A.R.,Correia, M.A.S.C.,Santos-Silva, T. (登録日: 2017-01-25, 公開日: 2017-08-02, 最終更新日: 2024-11-13)
主引用文献Otrelo-Cardoso, A.R.,Nair, R.R.,Correia, M.A.S.,Cordeiro, R.S.C.,Panjkovich, A.,Svergun, D.I.,Santos-Silva, T.,Rivas, M.G.
Highly selective tungstate transporter protein TupA from Desulfovibrio alaskensis G20.
Sci Rep, 7:5798-5798, 2017
Cited by
PubMed 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 MoO, WO 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.
PubMed: 28724964
DOI: 10.1038/s41598-017-06133-y
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.4 Å)
構造検証レポート
Validation report summary of 5my5
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-29に公開中

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