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Yorodumi- PDB-9ocj: Transporter associated with antigen processing (TAP) bound to the... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9ocj | |||||||||||||||||||||||||||
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| Title | Transporter associated with antigen processing (TAP) bound to the viral protein CPXV012 in the outward-facing open state | |||||||||||||||||||||||||||
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Keywords | MEMBRANE PROTEIN / ABC transporter / antigen processing / peptide transporter / immune evasion / poxvirus / cowpox | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationantigen processing and presentation of endogenous peptide antigen via MHC class Ib via ER pathway, TAP-dependent / tapasin binding / ABC-type peptide antigen transporter activity / ABC-type antigen peptide transporter / TAP complex / ABC-type peptide transporter activity / TAP2 binding / TAP1 binding / peptide antigen transport / MHC class Ib protein binding ...antigen processing and presentation of endogenous peptide antigen via MHC class Ib via ER pathway, TAP-dependent / tapasin binding / ABC-type peptide antigen transporter activity / ABC-type antigen peptide transporter / TAP complex / ABC-type peptide transporter activity / TAP2 binding / TAP1 binding / peptide antigen transport / MHC class Ib protein binding / cytosol to endoplasmic reticulum transport / peptide transport / peptide transmembrane transporter activity / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent / MHC class I protein binding / endoplasmic reticulum-Golgi intermediate compartment membrane / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / T cell mediated cytotoxicity / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / response to molecule of bacterial origin / MHC class I peptide loading complex / defense response / antigen processing and presentation of endogenous peptide antigen via MHC class I / ADP binding / positive regulation of T cell mediated cytotoxicity / transmembrane transport / centriolar satellite / peptide antigen binding / phagocytic vesicle membrane / protein transport / ER-Phagosome pathway / adaptive immune response / nuclear speck / endoplasmic reticulum membrane / endoplasmic reticulum / protein homodimerization activity / ATP hydrolysis activity / ATP binding / metal ion binding / membrane Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) Cowpox virus | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å | |||||||||||||||||||||||||||
Authors | Lee, J. / Manon, V. / Chen, J. | |||||||||||||||||||||||||||
| Funding support | United States, 2items
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Citation | Journal: To Be PublishedTitle: Transporter associated with antigen processing (TAP) bound to the viral protein CPXV012 in the outward-facing open state Authors: Lee, J. / Manon, V. / Chen, J. | |||||||||||||||||||||||||||
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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 | 9ocj.cif.gz | 248.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9ocj.ent.gz | 188.1 KB | Display | PDB format |
| PDBx/mmJSON format | 9ocj.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oc/9ocj ftp://data.pdbj.org/pub/pdb/validation_reports/oc/9ocj | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 70317MC 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: 75735.516 Da / Num. of mol.: 1 / Mutation: E632Q Source method: isolated from a genetically manipulated source Details: C-terminally fused to a TEV protease cut site and Spycatcher Source: (gene. exp.) Homo sapiens (human) / Gene: TAP2, ABCB3, PSF2, RING11, Y1 / Production host: Homo sapiens (human) / Strain (production host): HEK293 GnTI-References: UniProt: Q03519, ABC-type antigen peptide transporter | ||||||
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| #2: Protein | Mass: 13478.525 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: C-terminally fused to a TEV protease cut site, Spytag, a Precission protease site, and eGFP. Source: (gene. exp.) Cowpox virus / Gene: CPXV012 CDS / Production host: Homo sapiens (human) / Strain (production host): HEK293 GnTI- / References: UniProt: Q8QN49 | ||||||
| #3: Protein | Mass: 97399.672 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: C-terminally fused to a TEV protease cut site, Spytag, a Precission protease site, and eGFP. Source: (gene. exp.) Homo sapiens (human) / Gene: TAP1, ABCB2, PSF1, RING4, Y3 / Production host: Homo sapiens (human) / Strain (production host): HEK293 GnTI-References: UniProt: Q03518, ABC-type antigen peptide transporter | ||||||
| #4: Chemical | | #5: Chemical | Has ligand of interest | Y | 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: Ternary complex of the heterodimer TAP1 and TAP2 bound to the viral inhibitor CPXV012. Type: COMPLEX Details: TAP1 is C-terminally tagged with Spycatcher and CPXV012 is N-terminally tagged with GFP and Spytag Entity ID: #3, #1-#2 / Source: RECOMBINANT | |||||||||||||||||||||||||
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| Molecular weight | Value: 0.184 MDa / Experimental value: NO | |||||||||||||||||||||||||
| Source (natural) | Organism: Homo sapiens (human) | |||||||||||||||||||||||||
| Source (recombinant) | Organism: Homo sapiens (human) / Strain: HEK293S GnTI- | |||||||||||||||||||||||||
| Buffer solution | pH: 6.5 | |||||||||||||||||||||||||
| Buffer component |
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| Specimen | Conc.: 6 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: 279 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 defocus max: 2500 nm / Nominal defocus min: 800 nm / Alignment procedure: COMA FREE |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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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: 3395985 | ||||||||||||||||
| 3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 34592 / Symmetry type: POINT | ||||||||||||||||
| Refinement | Highest resolution: 3 Å / Cross valid method: NONE Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) |
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About Yorodumi



Homo sapiens (human)
Cowpox virus
United States, 2items
Citation
PDBj





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