TY  - JOUR
A1  - Schneider, Simon
A1  - Kühlbrandt, Werner
A1  - Yildiz, Özkan
T1  - Complementary structures of the yeast phosphate transporter Pho90 provide insights into its transport mechanism
T2  - Structure
N2  - Highlights
• Cryo-EM structures of the yeast low-affinity phosphate importer ScPho90
• Complementary structures reveal insights into the substrate translocation mechanism
• Comparisons with homologous transporters highlight the conserved transport mechanism
• Regulation by the SPX domain is discussed
Summary
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.
KW  - Cryo-EM
KW  - secondary transporter
KW  - phosphate transporter
KW  - phosphate homeostasis
KW  - phosphate transport regulation
KW  - phosphate translocation mechanism
KW  - membrane protein
Y1  - 2024
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/85522
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-855220
SN  - 0969-2126
VL  - 32
IS  - In Press, Corrected Proof
SP  - 1
EP  - 10
PB  - Elsevier
CY  - Amsterdam
ER  -