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Yorodumi- PDB-4v66: Structure of the E. coli ribosome and the tRNAs in Post-accommoda... -
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Basic information
| Entry | Database: PDB / ID: 4v66 | |||||||||
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| Title | Structure of the E. coli ribosome and the tRNAs in Post-accommodation state | |||||||||
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Keywords | RIBOSOME / translation / accommodation / tRNA selection | |||||||||
| Function / homology | Function and homology informationnegative regulation of cytoplasmic translational initiation / stringent response / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / positive regulation of ribosome biogenesis ...negative regulation of cytoplasmic translational initiation / stringent response / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / positive regulation of ribosome biogenesis / RNA-binding transcription regulator activity / translational termination / negative regulation of cytoplasmic translation / four-way junction DNA binding / DnaA-L2 complex / translation repressor activity / negative regulation of translational initiation / negative regulation of DNA-templated DNA replication initiation / mRNA regulatory element binding translation repressor activity / positive regulation of RNA splicing / assembly of large subunit precursor of preribosome / cytosolic ribosome assembly / regulation of DNA-templated transcription elongation / response to reactive oxygen species / ribosome assembly / transcription elongation factor complex / DNA endonuclease activity / transcription antitermination / regulation of cell growth / translational initiation / DNA-templated transcription termination / response to radiation / maintenance of translational fidelity / mRNA 5'-UTR binding / regulation of translation / large ribosomal subunit / ribosome biogenesis / ribosome binding / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / response to antibiotic / negative regulation of DNA-templated transcription / mRNA binding / DNA binding / RNA binding / zinc ion binding / membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() ![]() Sulfolobus acidocaldarius (acidophilic) | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 9 Å | |||||||||
Authors | Devkota, B. / Caulfield, T.R. / Tan, R.-Z. / Harvey, S.C. | |||||||||
Citation | Journal: To be PublishedTitle: The Structure of the E. coli Ribosome Before and After Accommodation: Implications for Proofreading Authors: Devkota, B. / Caulfield, T.R. / Tan, R.-Z. / Harvey, S.C. | |||||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 4v66.cif.gz | 3.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb4v66.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 4v66.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4v66_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
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| Full document | 4v66_full_validation.pdf.gz | 7.2 MB | Display | |
| Data in XML | 4v66_validation.xml.gz | 781.5 KB | Display | |
| Data in CIF | 4v66_validation.cif.gz | 1.1 MB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v6/4v66 ftp://data.pdbj.org/pub/pdb/validation_reports/v6/4v66 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 1056M ![]() 4v65C M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-RNA chain , 5 types, 7 molecules AAAPAEAMA1BABB
| #1: RNA chain | Mass: 24518.570 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() PDB-4V7W#2: RNA chain | | Mass: 6078.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() PDB-4V7W#3: RNA chain | | Mass: 495927.719 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() PDB-4V7W#24: RNA chain | | Mass: 37848.555 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #25: RNA chain | | Mass: 941306.188 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-30S ribosomal protein ... , 20 types, 20 molecules ABACADAFAGAHAIAJAKALANAOAQARASATAUAVAWAX
| #4: Protein | Mass: 26781.670 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #5: Protein | Mass: 13870.975 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #6: Protein | Mass: 13768.157 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #7: Protein | Mass: 13128.467 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #8: Protein | Mass: 11606.560 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein | Mass: 10319.882 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 9207.572 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #11: Protein | Mass: 9724.491 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #12: Protein | Mass: 9006.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #13: Protein | Mass: 10455.355 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #14: Protein | Mass: 9708.464 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #15: Protein | Mass: 26031.316 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #16: Protein | Mass: 8524.039 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #17: Protein | Mass: 23514.199 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #18: Protein | Mass: 16772.412 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #19: Protein | Mass: 15727.512 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #20: Protein | Mass: 20055.156 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #21: Protein | Mass: 14146.557 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #22: Protein | Mass: 14886.270 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #23: Protein | Mass: 11755.597 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+50S ribosomal protein ... , 30 types, 30 molecules BCBDBEBFBGBHBIBJBKBLBMBNBOBPBQBRBSBTBUBVBWBXBYBZB1B2B3B4B5B6
-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: E. coli ribosome in post-accommodation state / Type: RIBOSOME |
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| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Tecnai F20 / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TECNAI F20 |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 50000 X / Nominal defocus max: 4000 nm / Nominal defocus min: 2000 nm |
| Image recording | Electron dose: 15 e/Å2 / Film or detector model: KODAK SO-163 FILM |
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Processing
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| Symmetry | Point symmetry: C1 (asymmetric) | |||||||||||||||||||||
| 3D reconstruction | Method: Single Particle / Resolution: 9 Å / Num. of particles: 52181 / Nominal pixel size: 2.82 Å / Symmetry type: POINT | |||||||||||||||||||||
| Atomic model building | Protocol: FLEXIBLE FIT / Space: REAL / Target criteria: cross-correlation / Details: METHOD--Flexible fitting | |||||||||||||||||||||
| Atomic model building |
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| Refinement step | Cycle: LAST
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Sulfolobus acidocaldarius (acidophilic)
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