Structural basis of proton-coupled potassium transport in the KUP family
- 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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| Author: | Igor TascónORCiD, Joana Sofia de SousaORCiDGND, Robin A. CoreyORCiD, Deryck J. MillsORCiD, David Griwatz, Nadine Aumüller, Vedrana Mikusevic, Phillip J. StansfeldORCiD, Janet VonckORCiD, Inga HäneltORCiDGND |
|---|---|
| URN: | urn:nbn:de:hebis:30:3-528829 |
| DOI: | https://doi.org/10.1038/s41467-020-14441-7 |
| ISSN: | 2041-1723 |
| Pubmed Id: | https://pubmed.ncbi.nlm.nih.gov/32005818 |
| Parent Title (English): | Nature Communications |
| Publisher: | Nature Publishing Group UK |
| Place of publication: | [London] |
| Document Type: | Article |
| Language: | English |
| Year of Completion: | 2020 |
| Date of first Publication: | 2020/01/31 |
| Publishing Institution: | Universitätsbibliothek Johann Christian Senckenberg |
| Release Date: | 2020/02/19 |
| Tag: | Bacterial structural biology; Cryoelectron microscopy; Ion transport; Permeation and transport |
| Volume: | 11 |
| Issue: | 1, Art. 626 |
| Page Number: | 10 |
| First Page: | 1 |
| Last Page: | 10 |
| Note: | Open Access: This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
| HeBIS-PPN: | 460972197 |
| Institutes: | Biochemie, Chemie und Pharmazie / Biochemie und Chemie |
| Angeschlossene und kooperierende Institutionen / MPI für Biophysik | |
| Dewey Decimal Classification: | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
| Sammlungen: | Universitätspublikationen |
| Licence (German): |  Creative Commons - Namensnennung 4.0 |
