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| Title | Molecular architecture of the fungal-specific potassium channel TOK1. |
|---|---|
| Journal, issue, pages | Nat Commun, Year 2026 |
| Publish date | Apr 27, 2026 |
Authors | Brice Durocher / Rían W Manville / Rui Yan / Zhiheng Yu / Geoffrey W Abbott / Alexandria N Miller / ![]() |
| PubMed Abstract | In Candida albicans, potassium (K) channels fine-tune ionic balance under stress, contributing to host colonization. Fungal two-pore domain, outwardly rectifying potassium (TOK) channels remain ...In Candida albicans, potassium (K) channels fine-tune ionic balance under stress, contributing to host colonization. Fungal two-pore domain, outwardly rectifying potassium (TOK) channels remain insufficiently characterized despite evidence implicating them in growth and viability. Here, we describe the atomic-resolution structure of a fungal potassium channel, TOK1 from C. albicans (CaTOK), revealing an architecture defined by eight transmembrane helices and a membrane topology distinct from previously characterized K⁺ channel classes. The first four helices form a tetraspanin-like bundle resembling auxiliary subunits of human neuronal ion channels. The pore features an inner helical gating movement analogous to mammalian dimeric K channels, while the K selectivity filter exhibits atypical ion coordination. A cytosolic C-terminal bundle forms an intramolecular network that likely stabilizes CaTOK and may mediate gating. These findings provide a framework for understanding TOK channel function and facilitate future studies of fungal ion homeostasis, pathogenicity, and therapeutic development. |
External links | Nat Commun / PubMed:42045187 |
| Methods | EM (single particle) |
| Resolution | 2.62 - 3.05 Å |
| Structure data | EMDB-71670, PDB-9pik: EMDB-71702, PDB-9pko: EMDB-71703, PDB-9pkp: |
| Chemicals | ![]() ChemComp-K: ![]() ChemComp-LMT: |
| Source |
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Keywords | METAL TRANSPORT / potassium ion channel |
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candida albicans (yeast)
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