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Yorodumi- PDB-32qb: Cryo-EM structure of Saccharomyces cerevisiae Erv14-Qdr2 complex ... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 32qb | |||||||||
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| Title | Cryo-EM structure of Saccharomyces cerevisiae Erv14-Qdr2 complex in lipid nanodiscs (single Erv14 assembly) | |||||||||
Components |
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Keywords | MEMBRANE PROTEIN / Cargo Receptor / Cornichon / Major Facilitator Superfamily / Drug:Proton Antiporter / Erv14 / Qdr2 / Lipid-Mediated Interface | |||||||||
| Function / homology | Function and homology informationaxial cellular bud site selection / threonine efflux transmembrane transporter activity / amino acid export across plasma membrane / negative regulation of receptor localization to synapse / ascospore formation / copper ion export / regulation of AMPA receptor activity / COPII-coated ER to Golgi transport vesicle / monoatomic cation transmembrane transporter activity / cargo receptor activity ...axial cellular bud site selection / threonine efflux transmembrane transporter activity / amino acid export across plasma membrane / negative regulation of receptor localization to synapse / ascospore formation / copper ion export / regulation of AMPA receptor activity / COPII-coated ER to Golgi transport vesicle / monoatomic cation transmembrane transporter activity / cargo receptor activity / potassium ion import across plasma membrane / xenobiotic transmembrane transporter activity / endoplasmic reticulum to Golgi vesicle-mediated transport / transmembrane transporter activity / cell periphery / transmembrane transport / signaling receptor binding / Golgi membrane / endoplasmic reticulum membrane / endoplasmic reticulum / plasma membrane Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.85 Å | |||||||||
Authors | Adams, O. / Parker, J.L. / Newstead, S. | |||||||||
| Funding support | United Kingdom, 1items
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Citation | Journal: To Be PublishedTitle: Cornichon receptors couple membrane adaptation to cargo selection during ER export Authors: Tunyi, J. / Adams, O. / Forrest, L. / Parker, J.L. / Newstead, S. | |||||||||
| History |
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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 | 32qb.cif.gz | 140.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb32qb.ent.gz | 109.7 KB | Display | PDB format |
| PDBx/mmJSON format | 32qb.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/2q/32qb ftp://data.pdbj.org/pub/pdb/validation_reports/2q/32qb | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 59066MC ![]() 32pzC ![]() 32qaC 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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Components
| #1: Protein | Mass: 16940.873 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: ERV14, YGL054C / Production host: ![]() | ||||||||
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| #2: Protein | Mass: 60527.609 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: QDR2, YIL121W / Production host: ![]() | ||||||||
| #3: Chemical | ChemComp-Y01 / #4: Chemical | #5: Chemical | ChemComp-NKN / ( | Has ligand of interest | N | Has protein modification | N | |
-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: Saccharomyces cerevisiae Qdr2-Erv14 complex in lipid nanodiscs (single Erv14 assembly) Type: ORGANELLE OR CELLULAR COMPONENT / Entity ID: #1-#2 / Source: RECOMBINANT |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.5 / Details: 20 mM HEPES, 150 mM NaCl |
| Specimen | Conc.: 3.97 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: GOLD / Grid type: Quantifoil R1.2/1.3 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K |
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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 magnification: 105000 X / Nominal defocus max: 2200 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Average exposure time: 1.8 sec. / Electron dose: 40 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 49836 Details: First Collection = 15426 Images, Total Dose 40, 1.8 s Per Exposure Second Collection = 34410 Images, Total Dose 39.9, 1.8 s Per Exposure |
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Processing
| EM software |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 30817460 | ||||||||||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.85 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 168498 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||
| Atomic model building | Space: REAL |
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