6L85

The sodium-dependent phosphate transporter

6L85 の概要

• エントリーDOI: 10.2210/pdb6l85/pdb
• 分子名称: Phosphate transporter, PHOSPHATE ION, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: phosphate binding, sodium-dependent phosphate import, transport protein, membrane protein
• 由来する生物種: Thermotoga maritima MSB8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 88478.48

構造登録者

Tsai, J.-Y.,Sun, Y.-J. (登録日: 2019-11-04, 公開日: 2020-09-16, 最終更新日: 2024-03-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.302 Å)