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TitleStructural basis of urea transport by Arabidopsis thaliana DUR3.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 1782, Year 2025
Publish dateFeb 20, 2025
AuthorsWeidong An / Yiwei Gao / Laihua Liu / Qinru Bai / Jun Zhao / Yan Zhao / Xuejun C Zhang /
PubMed AbstractUrea 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 ...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.
External linksNat Commun / PubMed:39972035 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.0 Å
Structure data

61201

9j7c

EMDB-61201, PDB-9j7c:
Arabidopsis high-affinity urea transport DUR3 in the urea-bound occluded conformation, dimeric state
Method: EM (single particle) / Resolution: 3.0 Å

61202

9j7d

EMDB-61202, PDB-9j7d:
Arabidopsis high-affinity urea transport DUR3 in the inward-facing open conformation, dimeric state
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-URE:
UREA

ChemComp-R16:
HEXADECANE

ChemComp-C14:
TETRADECANE

ChemComp-HOH:
WATER

Source
  • arabidopsis thaliana (thale cress)
KeywordsMEMBRANE PROTEIN / DUR3 / high-affinity urea transporter / urea transporter

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