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Title | Complementary structures of the yeast phosphate transporter Pho90 provide insights into its transport mechanism. |
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Journal, issue, pages | Structure, Vol. 32, Issue 7, Page 979-988.e4, Year 2024 |
Publish date | Jul 11, 2024 |
Authors | Simon Schneider / Werner Kühlbrandt / Özkan Yildiz / |
PubMed Abstract | Phosphate homeostasis is essential for all living organisms. Low-affinity phosphate transporters are involved in phosphate import and regulation in a range of eukaryotic organisms. We have determined ...Phosphate homeostasis is essential for all living organisms. Low-affinity phosphate transporters are involved in phosphate import and regulation in a range of eukaryotic organisms. We have determined the structures of the Saccharomyces cerevisiae phosphate importer Pho90 by electron cryomicroscopy in two complementary states at 2.3 and 3.1 Å resolution. The symmetrical, outward-open structure in the presence of phosphate indicates bound substrate ions in the binding pocket. In the absence of phosphate, Pho90 assumes an asymmetric structure with one monomer facing inward and one monomer facing outward, providing insights into the transport mechanism. The Pho90 transport domain binds phosphate ions on one side of the membrane, then flips to the other side where the substrate is released. Together with functional experiments, these complementary structures illustrate the transport mechanism of eukaryotic low-affinity phosphate transporters. |
External links | Structure / PubMed:38688287 |
Methods | EM (single particle) |
Resolution | 2.29 - 3.12 Å |
Structure data | EMDB-18859, PDB-8r33: EMDB-18860, PDB-8r34: EMDB-18861, PDB-8r35: |
Chemicals | ChemComp-3PH: ChemComp-HOH: ChemComp-PO4: ChemComp-NA: |
Source |
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Keywords | MEMBRANE PROTEIN / Phosphate transporter / Plasma membrane protein |