Structural basis of urea transport by Arabidopsis thaliana DUR3

Weidong An, Yiwei Gao, Laihua Liu, Qinru Bai, Jun Zhao (), Yan Zhao () and Xuejun C. Zhang ()
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Weidong An: Shandong Laboratory of Advanced Agricultural Sciences at Weifang
Yiwei Gao: Chinese Academy of Sciences
Laihua Liu: China Agricultural University
Qinru Bai: Chinese Academy of Sciences
Jun Zhao: Shandong Laboratory of Advanced Agricultural Sciences at Weifang
Yan Zhao: Chinese Academy of Sciences
Xuejun C. Zhang: Chinese Academy of Sciences

Nature Communications, 2025, vol. 16, issue 1, 1-9

Abstract: 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.

Date: 2025
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DOI: 10.1038/s41467-025-56943-2

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