8R35

CryoEM structure of the asymmetric Pho90 dimer from yeast without substrates.

8R35 の概要

• エントリーDOI: 10.2210/pdb8r35/pdb
• EMDBエントリー: 18861
• 分子名称: Low-affinity phosphate transporter PHO90 (1 entity in total)
• 機能のキーワード: phosphate transporter, plasma membrane protein, membrane protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 195572.44

構造登録者

Schneider, S.,Kuehlbrandt, W.,Yildiz, O. (登録日: 2023-11-08, 公開日: 2024-04-24, 最終更新日: 2025-07-02)

主引用文献

Schneider, S.,Kuhlbrandt, W.,Yildiz, O.
Complementary structures of the yeast phosphate transporter Pho90 provide insights into its transport mechanism.
Structure, 32:979-, 2024

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: 38688287
DOI: 10.1016/j.str.2024.04.005

実験手法

ELECTRON MICROSCOPY (3.12 Å)