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TitleCryo-EM of the eukaryotic purine transporter UapA demonstrates intramolecular and lipid regulation of transport.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 123, Page e2513585123, Year 2026
Publish dateJun 1, 2026
AuthorsGeorge Broutzakis / Yiannis Pyrris / Ifigeneia Akrani / Alexander Neuhaus / Emmanuel Mikros / George Diallinas / Christos Gatsogiannis /
PubMed AbstractMembers of the nucleobase ascorbate transporter (NAT) family (SLC23) are elevator-type transporters that are responsible for the uptake of nucleobases and ascorbate. In fungi, NAT members are also ...Members of the nucleobase ascorbate transporter (NAT) family (SLC23) are elevator-type transporters that are responsible for the uptake of nucleobases and ascorbate. In fungi, NAT members are also responsible for the specific uptake of antifungal nucleobase analogues, such as oxypurinol, allopurinol, or 8-azaguanine. Here, we report nearly full-length cryo-EM structures of UapA, a high-affinity purine transporter from the model fungus , in inward-facing apo- and substrate-loaded conformations at 2.06 to 3.5 Å in detergent and lipid nanodiscs. The high-resolution structures reveal the role of water molecules and lipids in substrate binding, specificity, transporter dimerization, and activity. Notably, the N-tail of UapA is found to be structured, interacting with both the core and scaffold domains, which in combination with functional data suggests a dual role in trafficking and transport dynamics. Overall, our study provides unprecedented structural and functional insights into an elevator-type fungal transporter, which may well contribute to the exploitation of NAT transporters as specific gateways for targeted pharmacological antifungal approaches.
External linksProc. Natl. Acad. Sci. USA / PubMed:42361038 / PubMed Central
MethodsEM (single particle)
Resolution2.06 - 3.48 Å
Structure data

58351

31ew

EMDB-58351, PDB-31ew:
UapA (WT) in DDM, Apo state
Method: EM (single particle) / Resolution: 2.06 Å

58353

31ey

EMDB-58353, PDB-31ey:
UapA (Q408E) in DDM, Apo state
Method: EM (single particle) / Resolution: 2.59 Å

58354

31ez

EMDB-58354, PDB-31ez:
UapA (Q408E) in MSP1E3D1 nanodiscs, Xanthine-bound state
Method: EM (single particle) / Resolution: 3.48 Å

Chemicals

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

ChemComp-MYR:
MYRISTIC ACID

ChemComp-PLM:
PALMITIC ACID

ChemComp-ERG:
ERGOSTEROL

ChemComp-DAO:
LAURIC ACID

ChemComp-DGA:
DIACYL GLYCEROL

ChemComp-HOH:
WATER

ChemComp-FAW:
(2S)-3-hydroxypropane-1,2-diyl ditetradecanoate

ChemComp-XAN:
XANTHINE

Source
  • aspergillus nidulans fgsc a4 (mold)
KeywordsMEMBRANE PROTEIN / UapA / DDM / Transporter / Inward-facing / Uric Acid / Xanthine

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