9J7D

Arabidopsis high-affinity urea transport DUR3 in the inward-facing open conformation, dimeric state

9J7D の概要

• エントリーDOI: 10.2210/pdb9j7d/pdb
• EMDBエントリー: 61202
• 分子名称: Urea-proton symporter DUR3, CHOLESTEROL HEMISUCCINATE, TETRADECANE, ... (5 entities in total)
• 機能のキーワード: dur3, high-affinity urea transporter, urea transporter, membrane protein
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 154553.06

構造登録者

An, W.,Gao, Y.,Zhang, X.C. (登録日: 2024-08-18, 公開日: 2025-05-07)

主引用文献

An, W.,Gao, Y.,Liu, L.,Bai, Q.,Zhao, J.,Zhao, Y.,Zhang, X.C.
Structural basis of urea transport by Arabidopsis thaliana DUR3.
Nat Commun, 16:1782-1782, 2025

PubMed Abstract: Urea is a primary nitrogen source used as fertilizer in agricultural plant production and a crucial nitrogen metabolite in plants, playing an essential role in modern agriculture. In plants, DUR3 is a proton-driven high-affinity urea transporter located on the plasma membrane. It not only absorbs external low-concentration urea as a nutrient but also facilitates nitrogen transfer by recovering urea from senescent leaves. Despite its importance, the high-affinity urea transport mechanism in plants remains insufficiently understood. In this study, we determine the structures of Arabidopsis thaliana DUR3 in two different conformations: the inward-facing open state of the apo structure and the occluded urea-bound state, with overall resolutions of 2.8 Å and 3.0 Å, respectively. By comparing these structures and analyzing their functional characteristics, we elucidated how urea molecules are specifically recognized. In the urea-bound structure, we identified key titratable amino acid residues and proposed a model for proton involvement in urea transport based on structural and functional data. This study enhances our understanding of proton-driven urea transport mechanisms in DUR3.

PubMed: 39972035
DOI: 10.1038/s41467-025-56943-2

実験手法

ELECTRON MICROSCOPY (2.8 Å)