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Yorodumi- PDB-5tga: Crystal structure of the S.cerevisiae 80S ribosome in complex wit... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 5tga | |||||||||
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| Title | Crystal structure of the S.cerevisiae 80S ribosome in complex with the A-site bound aminoacyl-tRNA analog ACCA-Pro | |||||||||
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Keywords | RIBOSOME / translation / protein synthesis / proline / aminoacyl-tRNA / peptide bond formation / catalysis / cyclic amino acids | |||||||||
| Function / homology | Function and homology informationtriplex DNA binding / Platelet degranulation / ribosome hibernation / translation elongation factor binding / regulation of translational initiation in response to stress / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, LSU-rRNA,5S) / regulation of amino acid metabolic process / negative regulation of glucose mediated signaling pathway / positive regulation of translational fidelity / : ...triplex DNA binding / Platelet degranulation / ribosome hibernation / translation elongation factor binding / regulation of translational initiation in response to stress / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, LSU-rRNA,5S) / regulation of amino acid metabolic process / negative regulation of glucose mediated signaling pathway / positive regulation of translational fidelity / : / RMTs methylate histone arginines / Protein methylation / mTORC1-mediated signalling / Protein hydroxylation / ribosome-associated ubiquitin-dependent protein catabolic process / pre-mRNA 5'-splice site binding / GDP-dissociation inhibitor activity / positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / nonfunctional rRNA decay / Formation of the ternary complex, and subsequently, the 43S complex / Translation initiation complex formation / response to cycloheximide / Ribosomal scanning and start codon recognition / cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / preribosome, small subunit precursor / Major pathway of rRNA processing in the nucleolus and cytosol / mRNA destabilization / telomeric DNA binding / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / negative regulation of mRNA splicing, via spliceosome / preribosome, large subunit precursor / Formation of a pool of free 40S subunits / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / positive regulation of protein kinase activity / TOR signaling / negative regulation of translational frameshifting / L13a-mediated translational silencing of Ceruloplasmin expression / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / translational elongation / G-protein alpha-subunit binding / ribosomal large subunit export from nucleus / 90S preribosome / Ub-specific processing proteases / translational termination / regulation of translational fidelity / ribosomal subunit export from nucleus / protein-RNA complex assembly / maturation of LSU-rRNA / endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / translation repressor activity / translation regulator activity / ribosomal small subunit export from nucleus / DNA-(apurinic or apyrimidinic site) endonuclease activity / rescue of stalled cytosolic ribosome / telomere maintenance / cellular response to amino acid starvation / protein kinase C binding / ribosome assembly / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / macroautophagy / maturation of SSU-rRNA / translational initiation / small-subunit processome / maintenance of translational fidelity / modification-dependent protein catabolic process / protein tag activity / cytoplasmic stress granule / rRNA processing / ribosome biogenesis / ribosome binding / 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 / negative regulation of translation / rRNA binding / protein ubiquitination / structural constituent of ribosome / ribosome / translation / G protein-coupled receptor signaling pathway / negative regulation of gene expression / response to antibiotic / mRNA binding / ubiquitin protein ligase binding / negative regulation of apoptotic process / nucleolus / perinuclear region of cytoplasm / mitochondrion / DNA binding Similarity search - Function | |||||||||
| Biological species | ![]() synthetic construct (others) | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.3 Å | |||||||||
Authors | Melnikov, S. / Mailliot, J. | |||||||||
Citation | Journal: EMBO Rep. / Year: 2016Title: Molecular insights into protein synthesis with proline residues. Authors: Melnikov, S. / Mailliot, J. / Rigger, L. / Neuner, S. / Shin, B.S. / Yusupova, G. / Dever, T.E. / Micura, R. / Yusupov, M. | |||||||||
| 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 | 5tga.cif.gz | 10.2 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb5tga.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 5tga.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tg/5tga ftp://data.pdbj.org/pub/pdb/validation_reports/tg/5tga | HTTPS FTP |
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-Related structure data
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Links
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Assembly
| Deposited unit | ![]()
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| 2 | ![]()
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| Unit cell |
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Components
-18S ribosomal ... , 2 types, 2 molecules 26
| #1: RNA chain | Mass: 589169.000 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #80: RNA chain | Mass: 579761.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-40S ribosomal protein ... , 13 types, 26 molecules S0s0C3c3C7c7C8c8C9c9D1d1D2d2D3d3D4d4D6d6D7d7D8d8D9d9
| #2: Protein | Mass: 22811.074 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #15: Protein | Mass: 16928.748 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #19: Protein | Mass: 14268.545 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #20: Protein | Mass: 16940.443 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #21: Protein | Mass: 15810.930 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #23: Protein | Mass: 9758.829 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #24: Protein | Mass: 14518.867 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #25: Protein | Mass: 15942.699 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #26: Protein | Mass: 15231.650 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #28: Protein | Mass: 11022.989 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #29: Protein | Mass: 8762.195 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #30: Protein | Mass: 7116.281 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #31: Protein | Mass: 6335.303 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Small ribosomal subunit protein ... , 20 types, 38 molecules S1s1S2s2S3s3S4s4S6s6S7s7S8s8S9s9C0C1c1C2c2C4c4C5c5C6c6D0d0D5...
| #3: Protein | Mass: 24498.365 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 23212.979 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | Mass: 24702.791 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 29338.133 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | Mass: 25895.072 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | Mass: 21158.648 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | Mass: 22406.609 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | Mass: 21210.662 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | | Mass: 11571.100 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein | Mass: 17654.738 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein | Mass: 13327.331 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #16: Protein | Mass: 13560.528 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #17: Protein | Mass: 15232.891 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #18: Protein | Mass: 15746.292 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #22: Protein | Mass: 12575.547 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #27: Protein | Mass: 8001.377 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #32: Protein | Mass: 7006.346 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #33: Protein | Mass: 8703.462 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #34: Protein | Mass: 34710.023 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #81: Protein | | Mass: 11181.781 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Protein , 1 types, 2 molecules S5s5
| #7: Protein | Mass: 22908.338 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Suppressor protein STM1,Suppressor protein STM1,Suppressor protein STM1,Ribosome-bound protein ... , 2 types, 2 molecules SMsM
| #35: Protein | Mass: 16519.352 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #82: Protein | Mass: 10310.914 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-RNA chain , 4 types, 8 molecules 153748AB
| #36: RNA chain | Mass: 1096842.375 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #37: RNA chain | Mass: 38951.105 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #38: RNA chain | Mass: 50682.922 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #86: RNA chain | Mass: 893.627 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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+60S Ribosomal Protein ... , 35 types, 69 molecules L2l2L3l3L4l4L5l5L8l8L9l9M0m0M1m1M5m5M6m6M7m7M8m8M9m9N0n0N1n1...
-Large ribosomal subunit protein ... , 9 types, 17 molecules L6l6L7l7M3m3M4m4N4n4N6n6O0o0Q1q1p0
| #43: Protein | Mass: 19869.369 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #44: Protein | Mass: 25341.480 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #49: Protein | Mass: 21956.312 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #50: Protein | Mass: 15063.870 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #60: Protein | Mass: 15506.229 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #62: Protein | Mass: 14134.588 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #66: Protein | Mass: 10902.664 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #77: Protein/peptide | Mass: 3354.243 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #84: Protein | | Mass: 24044.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 4 types, 3555 molecules 






| #87: Chemical | ChemComp-OHX / #88: Chemical | ChemComp-MG / #89: Chemical | ChemComp-ZN / #90: Chemical | |
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-Details
| Has protein modification | Y |
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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: 3.17 Å3/Da / Density % sol: 61.19 % |
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| Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / Details: PEG20000 |
-Data collection
| Diffraction | Mean temperature: 277 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Diffraction source | Source: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 1 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Nov 1, 2014 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection | Resolution: 3.3→200 Å / Num. obs: 1026480 / % possible obs: 92.7 % / Observed criterion σ(I): -3 / Redundancy: 6 % / Biso Wilson estimate: 82.52 Å2 / CC1/2: 0.989 / Rmerge(I) obs: 0.333 / Net I/σ(I): 6.51 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection shell |
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-Phasing
| Phasing | Method: molecular replacement |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.3→149.313 Å / SU ML: 0.48 / Cross valid method: FREE R-VALUE / σ(F): 0 / Phase error: 26.95
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| Solvent computation | Shrinkage radii: 0.8 Å / VDW probe radii: 1.1 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso max: 231.38 Å2 / Biso mean: 73.4994 Å2 / Biso min: 21.63 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: final / Resolution: 3.3→149.313 Å
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| Refine LS restraints |
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| LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30
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