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Yorodumi- PDB-9q78: Crystal structure of T. cruzi EIF4E6 in complex with EIF4G5 peptide -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9q78 | |||||||||
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| Title | Crystal structure of T. cruzi EIF4E6 in complex with EIF4G5 peptide | |||||||||
Components |
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Keywords | TRANSLATION / TRANSLATION INITIATION FACTOR / EIF4E FAMILY / EIF4E6 / EIF4G5 | |||||||||
| Function / homology | Translation Initiation factor eIF- 4e-like / MIF4G domain / eukaryotic translation initiation factor 4F complex / MIF4G-like, type 3 / translation initiation factor activity / Armadillo-type fold / mRNA binding / Eukaryotic translation initiation factor 4 gamma 5 / Putative Eukaryotic translation initiation factor 4E type 6 Function and homology information | |||||||||
| Biological species | ![]() ![]() | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | |||||||||
Authors | Penteado, R.F. / Guimaraes, B.G. | |||||||||
| Funding support | France, Brazil, 2items
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Citation | Journal: J.Mol.Biol. / Year: 2026Title: Selective eIF4E-eIF4G Pairing and Cap-4 Recognition Mechanisms in Trypanosomatids: Insights From EIF4E5-EIF4G1 and EIF4E6-EIF4G5 Complexes. Authors: Penteado, R.F. / Vichier-Guerre, S. / da Silva Pereira, B.M. / Dugue, L. / Guerra Slompo, E.P. / Assuncao de Matos, T.R. / Pochet, S. / Zanchin, N.I.T. / Guimaraes, B.G. | |||||||||
| 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 | 9q78.cif.gz | 339.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9q78.ent.gz | 276.1 KB | Display | PDB format |
| PDBx/mmJSON format | 9q78.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q7/9q78 ftp://data.pdbj.org/pub/pdb/validation_reports/q7/9q78 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 9q72C ![]() 9q73C ![]() 9q74C ![]() 9q75C ![]() 9q79C 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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| 2 | ![]()
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| 3 | ![]()
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| 4 | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 21401.348 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Protein/peptide | Mass: 5706.448 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #3: Water | ChemComp-HOH / | Has protein modification | N | |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 2.05 Å3/Da / Density % sol: 40.1 % |
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| Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop Details: Complex at 7.3 mg/mL in 20 mM Tris-HCl, 150 mM NaCl, 2 mM DTT, pH 8.0 with crystallization buffer containing 80 mM Monosaccharides (0.2 M D-glucose, 0.2 M D-mannose, 0.2 M D-galactose, 0.2 M ...Details: Complex at 7.3 mg/mL in 20 mM Tris-HCl, 150 mM NaCl, 2 mM DTT, pH 8.0 with crystallization buffer containing 80 mM Monosaccharides (0.2 M D-glucose, 0.2 M D-mannose, 0.2 M D-galactose, 0.2 M L-fucose, 0.2 M D-xylose, 0.2 M N-acetyl-D-glucosamine), 100 mM Buffer System 1 (pH 6.5; 0.4 M imidazole, 0.6 M MES monohydrate), and 37.5% (w/v) Precipitant Mix 4 (25% v/v MPD, 25% v/v PEG 1000, 25% w/v PEG 3350) |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.97856 Å |
| Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 19, 2024 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.97856 Å / Relative weight: 1 |
| Reflection | Resolution: 2.1→112.69 Å / Num. obs: 37674 / % possible obs: 94.4 % / Redundancy: 7 % / CC1/2: 0.997 / Net I/σ(I): 7.5 |
| Reflection shell | Resolution: 2.1→2.19 Å / Num. unique obs: 1884 / CC1/2: 0.767 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.1→49.58 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.892 / SU B: 18.676 / SU ML: 0.21 / Cross valid method: THROUGHOUT / ESU R Free: 0.276 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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| Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 15.359 Å2
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| Refinement step | Cycle: 1 / Resolution: 2.1→49.58 Å
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| Refine LS restraints |
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X-RAY DIFFRACTION
France,
Brazil, 2items
Citation




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