6L85

The sodium-dependent phosphate transporter

Summary for 6L85

• Entry DOI: 10.2210/pdb6l85/pdb
• Descriptor: Phosphate transporter, PHOSPHATE ION, SODIUM ION, ... (6 entities in total)
• Functional Keywords: phosphate binding, sodium-dependent phosphate import, transport protein, membrane protein
• Biological source: Thermotoga maritima MSB8
• Total number of polymer chains: 2
• Total formula weight: 88478.48

Authors

Tsai, J.-Y.,Sun, Y.-J. (deposition date: 2019-11-04, release date: 2020-09-16, Last modification date: 2024-03-27)

Primary citation

Tsai, J.-Y.,Chu, C.-H.,Lin, M.-G.,Chou, Y.-H.,Hong, R.-Y.,Yen, C.-Y.,Hsiao, C.-D.,Sun, Y.-J.
Structure of the sodium-dependent phosphate transporter reveals insights into human solute carrier SLC20.
Sci Adv, 6:eabb4024-eabb4024, 2020

PubMed Abstract: Inorganic phosphate (P) is a fundamental and essential element for nucleotide biosynthesis, energy supply, and cellular signaling in living organisms. Human phosphate transporter (PiT) dysfunction causes numerous diseases, but the molecular mechanism underlying transporters remains elusive. We report the structure of the sodium-dependent phosphate transporter from (PiT) in complex with sodium and phosphate (PiT-Na/Pi) at 2.3-angstrom resolution. We reveal that one phosphate and two sodium ions (Pi-2Na) are located at the core of PiT and that the third sodium ion (Na) is located near the inner membrane boundary. We propose an elevator-like mechanism for sodium and phosphate transport by PiT, with the PiT-Na/Pi complex adopting an inward occluded conformation. We found that disease-related PiT variants carry mutations in the corresponding sodium- and phosphate-binding residues identified in PiT. Our three-dimensional structure of PiT provides a framework for understanding PiT dysfunction and for future structure-based drug design.

PubMed: 32821837
DOI: 10.1126/sciadv.abb4024

Experimental method

X-RAY DIFFRACTION (2.302 Å)