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Yorodumi- PDB-4v85: Crystal Structure of Release Factor RF3 Trapped in the GTP State ... -
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-Basic information
Entry | Database: PDB / ID: 4v85 | |||||||||
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Title | Crystal Structure of Release Factor RF3 Trapped in the GTP State on a Rotated Conformation of the Ribosome. | |||||||||
Components |
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Keywords | RIBOSOME/ANTIBIOTIC / typeII release factor binding with ribosome / RIBOSOME-ANTIBIOTIC complex | |||||||||
Function / homology | Function and homology information regulation of translational termination / translation release factor activity, codon nonspecific / translation release factor activity, codon specific / 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 nonspecific / translation release factor activity, codon specific / 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 / RNA-binding transcription regulator activity / positive regulation of ribosome biogenesis / negative regulation of cytoplasmic translation / four-way junction DNA binding / translational termination / DnaA-L2 complex / translation repressor activity / negative regulation of DNA-templated DNA replication initiation / negative regulation of translational initiation / regulation of mRNA stability / mRNA regulatory element binding translation repressor activity / ribosome assembly / assembly of large subunit precursor of preribosome / positive regulation of RNA splicing / transcription elongation factor complex / cytosolic ribosome assembly / regulation of DNA-templated transcription elongation / DNA endonuclease activity / response to reactive oxygen species / transcription antitermination / regulation of cell growth / DNA-templated transcription termination / maintenance of translational fidelity / response to radiation / mRNA 5'-UTR binding / GDP binding / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / large ribosomal subunit / ribosome biogenesis / ribosome binding / regulation of translation / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / large ribosomal subunit rRNA binding / transferase activity / cytosolic small ribosomal subunit / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit / tRNA binding / molecular adaptor activity / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / ribonucleoprotein complex / 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 | Escherichia coli (E. coli) Streptomyces (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å | |||||||||
Authors | Zhou, J. / Lancaster, L. / Trakhanov, S. / Noller, H.F. | |||||||||
Citation | Journal: Rna / Year: 2012 Title: 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. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4v85.cif.gz | 3.7 MB | Display | PDBx/mmCIF format |
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PDB format | pdb4v85.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 4v85.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4v85_validation.pdf.gz | 1.5 MB | Display | wwPDB validaton report |
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Full document | 4v85_full_validation.pdf.gz | 2.4 MB | Display | |
Data in XML | 4v85_validation.xml.gz | 432.9 KB | Display | |
Data in CIF | 4v85_validation.cif.gz | 614.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v8/4v85 ftp://data.pdbj.org/pub/pdb/validation_reports/v8/4v85 | HTTPS FTP |
-Related structure data
-Links
-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 / References: GenBank: 323376397 |
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#22: RNA chain | Mass: 8862.456 Da / Num. of mol.: 1 / Source method: obtained synthetically |
#34: RNA chain | Mass: 941306.188 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: GenBank: 315134697 |
#35: RNA chain | Mass: 38177.762 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: GenBank: 323376397 |
-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) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3TPN2, UniProt: P0A7V0*PLUS |
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#3: Protein | Mass: 26031.316 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3SQX2, UniProt: P0A7V3*PLUS |
#4: Protein | Mass: 23514.199 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3SR62, UniProt: P0A7V8*PLUS |
#5: Protein | Mass: 17629.398 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3SR27, UniProt: P0A7W1*PLUS |
#6: Protein | Mass: 15211.058 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3SFQ7, UniProt: P02358*PLUS |
#7: Protein | Mass: 17637.445 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3SQS2, UniProt: P02359*PLUS |
#8: Protein | Mass: 14146.557 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3SR12, UniProt: P0A7W7*PLUS |
#9: Protein | Mass: 14886.270 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3SRY2, UniProt: P0A7X3*PLUS |
#10: Protein | Mass: 11755.597 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3SQT7, UniProt: P0A7R5*PLUS |
#11: Protein | Mass: 13870.975 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3SR57, UniProt: P0A7R9*PLUS |
#12: Protein | Mass: 13768.157 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3SQR7, UniProt: P0A7S3*PLUS |
#13: Protein | Mass: 13128.467 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3SR52, UniProt: P0A7S9*PLUS |
#14: Protein | Mass: 11606.560 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3SR07, UniProt: P0AG59*PLUS |
#15: Protein | Mass: 10290.816 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3SSQ7, UniProt: P0ADZ4*PLUS |
#16: Protein | Mass: 9207.572 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3SYP2, UniProt: P0A7T3*PLUS |
#17: Protein | Mass: 9724.491 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3SQY7, UniProt: P0AG63*PLUS |
#18: Protein | Mass: 9005.472 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3SFP7, UniProt: P0A7T7*PLUS |
#19: Protein | Mass: 10455.355 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3SQW2, UniProt: P0A7U3*PLUS |
#20: Protein | Mass: 9708.464 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: P0A7U7 |
#21: Protein | Mass: 8524.039 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: CSH142 / References: UniProt: C3STZ7, UniProt: P68679*PLUS |
+50S ribosomal protein ... , 30 types, 33 molecules B0B1B2B3B4B5B6B7B8BCBDBEBFBGBHBIBJBKBLBMBNBOBPBQBRBSBTBUBVBW...
-Protein / Protein/peptide , 2 types, 2 molecules AWAY
#23: Protein | Mass: 59651.934 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: MRE600 Gene: b4375, JW5873, miaD, prfC, Termination Release Factor 3, tos Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P0A7I4 |
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#24: Protein/peptide | |
-Non-polymers , 3 types, 511 molecules
#57: Chemical | ChemComp-MG / #58: Chemical | ChemComp-GNP / | #59: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 4 |
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-Sample preparation
Crystal | Density Matthews: 2.93 Å3/Da / Density % sol: 57.99 % |
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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: APS / Beamline: 23-ID-D / Wavelength: 1.03318 Å |
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Apr 2, 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: 3.2→50 Å / Num. obs: 433307 / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.2→40 Å / σ(F): 1.99 / σ(I): 1.71 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 3.2→40 Å
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Refine LS restraints |
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