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-Structure paper
タイトル | Structural basis of proton-coupled potassium transport in the KUP family. |
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ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 626, Year 2020 |
掲載日 | 2020年1月31日 |
![]() | Igor Tascón / Joana S Sousa / Robin A Corey / Deryck J Mills / David Griwatz / Nadine Aumüller / Vedrana Mikusevic / Phillip J Stansfeld / Janet Vonck / Inga Hänelt / ![]() ![]() |
PubMed 要旨 | Potassium homeostasis is vital for all organisms, but is challenging in single-celled organisms like bacteria and yeast and immobile organisms like plants that constantly need to adapt to changing ...Potassium homeostasis is vital for all organisms, but is challenging in single-celled organisms like bacteria and yeast and immobile organisms like plants that constantly need to adapt to changing external conditions. KUP transporters facilitate potassium uptake by the co-transport of protons. Here, we uncover the molecular basis for transport in this widely distributed family. We identify the potassium importer KimA from Bacillus subtilis as a member of the KUP family, demonstrate that it functions as a K/H symporter and report a 3.7 Å cryo-EM structure of the KimA homodimer in an inward-occluded, trans-inhibited conformation. By introducing point mutations, we identify key residues for potassium and proton binding, which are conserved among other KUP proteins. |
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手法 | EM (単粒子) |
解像度 | 3.7 Å |
構造データ | EMDB-10092, PDB-6s3k: |
化合物 | ![]() ChemComp-K: |
由来 |
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![]() | TRANSPORT PROTEIN / potassium transporter / LeuT fold / symporter / SMALP |