8R35
CryoEM structure of the asymmetric Pho90 dimer from yeast without substrates.
Summary for 8R35
| Entry DOI | 10.2210/pdb8r35/pdb |
| EMDB information | 18861 |
| Descriptor | Low-affinity phosphate transporter PHO90 (1 entity in total) |
| Functional Keywords | phosphate transporter, plasma membrane protein, membrane protein |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 195572.44 |
| Authors | Schneider, S.,Kuehlbrandt, W.,Yildiz, O. (deposition date: 2023-11-08, release date: 2024-04-24, Last modification date: 2024-07-24) |
| Primary citation | Schneider, S.,Kuhlbrandt, W.,Yildiz, O. Complementary structures of the yeast phosphate transporter Pho90 provide insights into its transport mechanism. Structure, 32:979-, 2024 Cited by 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 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. PubMed: 38688287DOI: 10.1016/j.str.2024.04.005 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.12 Å) |
Structure validation
Download full validation report
