9J7C
Arabidopsis high-affinity urea transport DUR3 in the urea-bound occluded conformation, dimeric state
Summary for 9J7C
| Entry DOI | 10.2210/pdb9j7c/pdb |
| EMDB information | 61201 |
| Descriptor | Urea-proton symporter DUR3, CHOLESTEROL HEMISUCCINATE, UREA, ... (6 entities in total) |
| Functional Keywords | dur3, high-affinity urea transporter, urea transporter, membrane protein |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 2 |
| Total formula weight | 154673.17 |
| Authors | |
| Primary citation | 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 Cited by 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: 39972035DOI: 10.1038/s41467-025-56943-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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