Structural basis of proton-coupled potassium transport in the KUP family
| Autor: | David Griwatz, Robin A. Corey, Phillip J. Stansfeld, Deryck J. Mills, Inga Hänelt, Joana S. Sousa, Vedrana Mikusevic, Nadine Aumüller, Igor Tascón, Janet Vonck |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Models
Molecular 0301 basic medicine Proton binding Potassium Science 030106 microbiology Protein domain General Physics and Astronomy chemistry.chemical_element Bacillus subtilis Article General Biochemistry Genetics and Molecular Biology 03 medical and health sciences Bacterial Proteins Protein Domains Cryoelectron microscopy ddc:570 QD lcsh:Science Cation Transport Proteins Ion transporter Bacterial structural biology Binding Sites Ion Transport Multidisciplinary biology Biological Transport General Chemistry biology.organism_classification QR Transport protein 030104 developmental biology Kima Biochemistry chemistry Multigene Family Symporter Permeation and transport lcsh:Q Dimerization |
| Zdroj: | Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020) Nature Communications |
| ISSN: | 2041-1723 |
| Popis: | 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. KUP transporters facilitate potassium uptake by the co-transport of protons and are key players in potassium homeostasis. Here authors identify the potassium importer KimA from Bacillus subtilis as a new member of the KUP transporter family and show the cryo-EM structure of KimA in an inward-occluded, trans-inhibited conformation. |
| Databáze: | OpenAIRE |
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