{"entity": "publication", "iuid": "4382ecc4480b47d6b762a8655bc6482e", "timestamp": "2026-09-25T23:03:31.052Z", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/4382ecc4480b47d6b762a8655bc6482e.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/4382ecc4480b47d6b762a8655bc6482e"}}, "title": "Structure and mechanism of the K+/H+ exchanger KefC.", "authors": [{"family": "Gulati", "given": "Ashutosh", "initials": "A", "orcid": "0000-0003-0960-994X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/084ce4065c7d4172969dd9aa2600790b.json"}}, {"family": "Kokane", "given": "Surabhi", "initials": "S"}, {"family": "Perez-Boerema", "given": "Annemarie", "initials": "A"}, {"family": "Alleva", "given": "Claudia", "initials": "C", "orcid": "0000-0001-8595-9250", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9507e83a9f924c83832d047c6db02906.json"}}, {"family": "Meier", "given": "Pascal F", "initials": "PF"}, {"family": "Matsuoka", "given": "Rei", "initials": "R"}, {"family": "Drew", "given": "David", "initials": "D", "orcid": "0000-0001-8866-6349", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e80593c5f1ec4f87a38b079e5909f0b0.json"}}], "type": "journal article", "published": "2024-06-04", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "15", "issue": "1", "pages": "4751", "issn-l": "2041-1723"}, "abstract": "Intracellular potassium (K+) homeostasis is fundamental to cell viability. In addition to channels, K+ levels are maintained by various ion transporters. One major family is the proton-driven K+ efflux transporters, which in gram-negative bacteria is important for detoxification and in plants is critical for efficient photosynthesis and growth. Despite their importance, the structure and molecular basis for K+-selectivity is poorly understood. Here, we report ~3.1 \u00c5 resolution cryo-EM structures of the Escherichia coli glutathione (GSH)-gated K+ efflux transporter KefC in complex with AMP, AMP/GSH and an ion-binding variant. KefC forms a homodimer similar to the inward-facing conformation of Na+/H+ antiporter NapA. By structural assignment of a coordinated K+ ion, MD simulations, and SSM-based electrophysiology, we demonstrate how ion-binding in KefC is adapted for binding a dehydrated K+ ion. KefC harbors C-terminal regulator of K+ conductance (RCK) domains, as present in some bacterial K+-ion channels. The domain-swapped helices in the RCK domains bind AMP and GSH and they inhibit transport by directly interacting with the ion-transporter module. Taken together, we propose that KefC is activated by detachment of the RCK domains and that ion selectivity exploits the biophysical properties likewise adapted by K+-ion-channels.", "doi": "10.1038/s41467-024-49082-7", "pmid": "38834573", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11150392"}, {"db": "pii", "key": "10.1038/s41467-024-49082-7"}], "notes": [], "created": "2026-09-23T11:27:37.307Z", "modified": "2026-09-23T11:27:37.391Z"}