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Yorodumi- PDB-4v89: Crystal Structure of Release Factor RF3 Trapped in the GTP State ... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 4v89 | |||||||||
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| Title | Crystal Structure of Release Factor RF3 Trapped in the GTP State on a Rotated Conformation of the Ribosome (without viomycin) | |||||||||
Components |
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Keywords | RIBOSOME / typeII release factor binding with ribosome | |||||||||
| Function / homology | Function and homology informationregulation of translational termination / translation release factor activity, codon specific / translation release factor activity, codon nonspecific / guanosine tetraphosphate binding / stringent response / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding ...regulation of translational termination / translation release factor activity, codon specific / translation release factor activity, codon nonspecific / guanosine tetraphosphate binding / 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 / regulation of mRNA stability / 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 / DNA-templated transcription termination / response to radiation / maintenance of translational fidelity / mRNA 5'-UTR binding / GDP 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 / response to antibiotic / negative regulation of DNA-templated transcription / GTPase activity / mRNA binding / GTP binding / protein homodimerization activity / DNA binding / RNA binding / zinc ion binding / membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.7 Å | |||||||||
Authors | Zhou, J. / Lancaster, L. / Trakhanov, S. / Noller, H.F. | |||||||||
Citation | Journal: Rna / Year: 2012Title: Crystal structure of release factor RF3 trapped in the GTP state on a rotated conformation of the ribosome. Authors: Zhou, J. / Lancaster, L. / Trakhanov, S. / Noller, H.F. | |||||||||
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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 | 4v89.cif.gz | 3.7 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb4v89.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 4v89.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4v89_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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| Full document | 4v89_full_validation.pdf.gz | 1.7 MB | Display | |
| Data in XML | 4v89_validation.xml.gz | 396.3 KB | Display | |
| Data in CIF | 4v89_validation.cif.gz | 544.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v8/4v89 ftp://data.pdbj.org/pub/pdb/validation_reports/v8/4v89 | HTTPS FTP |
-Related structure data
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Unit cell |
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Components
-RNA chain , 4 types, 4 molecules AAAVBABB
| #1: RNA chain | Mass: 496892.375 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #22: RNA chain | Mass: 8862.456 Da / Num. of mol.: 1 / Source method: obtained synthetically |
| #33: RNA chain | Mass: 941306.188 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #34: RNA chain | Mass: 38177.762 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-30S ribosomal protein ... , 20 types, 20 molecules ABACADAEAFAGAHAIAJAKALAMANAOAPAQARASATAU
| #2: Protein | Mass: 26781.670 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #3: Protein | Mass: 26031.316 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #4: Protein | Mass: 23514.199 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #5: Protein | Mass: 17629.398 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #6: Protein | Mass: 15727.512 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #7: Protein | Mass: 20055.156 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #8: Protein | Mass: 14146.557 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein | Mass: 14886.270 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 11755.597 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #11: Protein | Mass: 13870.975 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #12: Protein | Mass: 13768.157 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #13: Protein | Mass: 13128.467 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #14: Protein | Mass: 11606.560 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #15: Protein | Mass: 10290.816 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #16: Protein | Mass: 9207.572 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #17: Protein | Mass: 9724.491 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #18: Protein | Mass: 9005.472 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #19: Protein | Mass: 10455.355 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #20: Protein | Mass: 9708.464 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #21: Protein | Mass: 8524.039 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 1 types, 1 molecules AW
| #23: Protein | Mass: 60342.680 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: b4375, JW5873, miaD, prfC, Termination Release Factor 3, tos Production host: ![]() |
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+50S ribosomal protein ... , 30 types, 33 molecules B0B1B2B3B4B5B6B7B8BCBDBEBFBGBHBIBJBKBLBMBNBOBPBQBRBSBTBUBVBW...
-Non-polymers , 2 types, 2 molecules 


| #56: Chemical | ChemComp-GNP / |
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| #57: Chemical | ChemComp-MG / |
-Details
| Has protein modification | Y |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 2.96 Å3/Da / Density % sol: 58.45 % |
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| Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 7 Details: Tris Ac PH.7.0 25-35 mM KCL 6.1% PEG 20000 %1 glycerol 50mM sucrose , VAPOR DIFFUSION, SITTING DROP, temperature 295K |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 12.3.1 / Wavelength: 1.03318 Å |
| Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: May 1, 2011 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1.03318 Å / Relative weight: 1 |
| Reflection | Resolution: 3.7→50 Å / Num. obs: 329524 / % possible obs: 99.5 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.7→40 Å / σ(F): 2 / σ(I): 1.45 / Stereochemistry target values: Engh & Huber
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| Refinement step | Cycle: LAST / Resolution: 3.7→40 Å
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| Refine LS restraints |
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