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Open data
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Basic information
| Entry | Database: PDB / ID: 31ey | ||||||||||||||||||||||||||||||
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| Title | UapA (Q408E) in DDM, Apo state | ||||||||||||||||||||||||||||||
Components | Uric acid-xanthine permease | ||||||||||||||||||||||||||||||
Keywords | MEMBRANE PROTEIN / UapA / DDM / Transporter / Inward-facing / Uric Acid / Xanthine | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationxanthine transport / xanthine transmembrane transporter activity / autophagosome lumen / purine nucleobase binding / urate transport / urate transmembrane transporter activity / fungal-type vacuole / endosome membrane / plasma membrane Similarity search - Function | ||||||||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.59 Å | ||||||||||||||||||||||||||||||
Authors | Broutzakis, G. / Gatsogiannis, C. | ||||||||||||||||||||||||||||||
| Funding support | Germany, 2items
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Citation | Journal: Proc Natl Acad Sci U S A / Year: 2026Title: Cryo-EM of the eukaryotic purine transporter UapA demonstrates intramolecular and lipid regulation of transport. Authors: George Broutzakis / Yiannis Pyrris / Ifigeneia Akrani / Alexander Neuhaus / Emmanuel Mikros / George Diallinas / Christos Gatsogiannis / ![]() Abstract: 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 ...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. | ||||||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 31ey.cif.gz | 241.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb31ey.ent.gz | 196.6 KB | Display | PDB format |
| PDBx/mmJSON format | 31ey.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/1e/31ey ftp://data.pdbj.org/pub/pdb/validation_reports/1e/31ey | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 58353MC ![]() 31ewC ![]() 31ezC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
-Protein / Sugars , 2 types, 16 molecules AB

| #1: Protein | Mass: 55253.984 Da / Num. of mol.: 2 / Mutation: Q408E Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Sugar | ChemComp-LMT / |
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-Non-polymers , 6 types, 148 molecules 










| #3: Chemical | ChemComp-MYR / #4: Chemical | ChemComp-PLM / #5: Chemical | ChemComp-ERG / #6: Chemical | ChemComp-DAO / #7: Chemical | ChemComp-FAW / ( #8: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: UapA (WT) in DDM, Apo state / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT | ||||||||||||||||||||
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| Molecular weight | Value: 0.12 MDa / Experimental value: NO | ||||||||||||||||||||
| Source (natural) | Organism: ![]() | ||||||||||||||||||||
| Source (recombinant) | Organism: ![]() | ||||||||||||||||||||
| Buffer solution | pH: 7.5 | ||||||||||||||||||||
| Buffer component |
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| Specimen | Conc.: 5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 286.15 K Details: Vitrification chamber was allowed to equilibrate for 15 min at 100% humidity. |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2200 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.59 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 180198 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 2.59 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi






Germany, 2items
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FIELD EMISSION GUN