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Open data
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Basic information
| Entry | Database: PDB / ID: 7zw0 | ||||||||||||
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| Title | FAP-80S Complex - Rotated state | ||||||||||||
Components |
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Keywords | RIBOSOME / NRD / Ubiquitination / E3 ligase / Quality Control System | ||||||||||||
| Function / homology | Function and homology informationregulation of homoserine biosynthetic process / Calcineurin activates NFAT / negative regulation of homoserine biosynthetic process / regulation of protein folding / macrolide binding / 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 / translational readthrough / positive regulation of translational fidelity ...regulation of homoserine biosynthetic process / Calcineurin activates NFAT / negative regulation of homoserine biosynthetic process / regulation of protein folding / macrolide binding / 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 / translational readthrough / positive regulation of translational fidelity / RMTs methylate histone arginines / Protein methylation / response to cycloheximide / mTORC1-mediated signalling / Protein hydroxylation / pre-mRNA 5'-splice site binding / GDP-dissociation inhibitor activity / cytosolic large ribosomal subunit assembly / Ribosome Quality Control (RQC) complex extracts and degrades nascent peptide / ascospore wall assembly / Formation of the ternary complex, and subsequently, the 43S complex / Translation initiation complex formation / Ribosomal scanning and start codon recognition / positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / nonfunctional rRNA decay / preribosome, small subunit precursor / cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / mRNA destabilization / Major pathway of rRNA processing in the nucleolus and cytosol / PELO:HBS1L and ABCE1 dissociate a ribosome on a non-stop mRNA / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / Formation of a pool of free 40S subunits / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / preribosome, large subunit precursor / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / positive regulation of protein kinase activity / L13a-mediated translational silencing of Ceruloplasmin expression / negative regulation of mRNA splicing, via spliceosome / negative regulation of translational frameshifting / translational elongation / ribosomal large subunit export from nucleus / G-protein alpha-subunit binding / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / 90S preribosome / ribosomal subunit export from nucleus / translational termination / regulation of translational fidelity / maturation of LSU-rRNA / protein-RNA complex assembly / ribosome-associated ubiquitin-dependent protein catabolic process / 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 regulator activity / ribosomal small subunit export from nucleus / DNA-(apurinic or apyrimidinic site) endonuclease activity / protein folding chaperone / cellular response to amino acid starvation / protein kinase C binding / rescue of stalled cytosolic ribosome / macroautophagy / ribosomal large subunit biogenesis / ribosome assembly / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / maturation of SSU-rRNA / small-subunit processome / translational initiation / maintenance of translational fidelity / modification-dependent protein catabolic process / transcription by RNA polymerase II / cytoplasmic stress granule / protein tag activity / rRNA processing / cytosolic ribosome / ribosomal small subunit assembly / ribosome binding / ribosomal small subunit biogenesis / ribosome biogenesis / protein folding / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / DNA-binding transcription activator activity, RNA polymerase II-specific / chromatin organization / cytosolic large ribosomal subunit / nucleic acid binding / cytoplasmic translation / negative regulation of translation / protein ubiquitination / rRNA binding / ribosome / translation / DNA-binding transcription factor activity / structural constituent of ribosome / G protein-coupled receptor signaling pathway Similarity search - Function | ||||||||||||
| Biological species | ![]() | ||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.4 Å | ||||||||||||
Authors | Ikeuchi, K. / Buschauer, R. / Berninghausen, O. / Becker, T. / Beckmann, R. | ||||||||||||
| Funding support | Germany, European Union, 3items
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Citation | Journal: Mol Cell / Year: 2022Title: Sensing of individual stalled 80S ribosomes by Fap1 for nonfunctional rRNA turnover. Authors: Sihan Li / Ken Ikeuchi / Misaki Kato / Robert Buschauer / Takato Sugiyama / Shungo Adachi / Hideo Kusano / Tohru Natsume / Otto Berninghausen / Yoshitaka Matsuo / Thomas Becker / Roland ...Authors: Sihan Li / Ken Ikeuchi / Misaki Kato / Robert Buschauer / Takato Sugiyama / Shungo Adachi / Hideo Kusano / Tohru Natsume / Otto Berninghausen / Yoshitaka Matsuo / Thomas Becker / Roland Beckmann / Toshifumi Inada / ![]() Abstract: Cells can respond to stalled ribosomes by sensing ribosome collisions and employing quality control pathways. How ribosome stalling is resolved without collisions, however, has remained elusive. ...Cells can respond to stalled ribosomes by sensing ribosome collisions and employing quality control pathways. How ribosome stalling is resolved without collisions, however, has remained elusive. Here, focusing on noncolliding stalling exhibited by decoding-defective ribosomes, we identified Fap1 as a stalling sensor triggering 18S nonfunctional rRNA decay via polyubiquitination of uS3. Ribosome profiling revealed an enrichment of Fap1 at the translation initiation site but also an association with elongating individual ribosomes. Cryo-EM structures of Fap1-bound ribosomes elucidated Fap1 probing the mRNA simultaneously at both the entry and exit channels suggesting an mRNA stasis sensing activity, and Fap1 sterically hinders the formation of canonical collided di-ribosomes. Our findings indicate that individual stalled ribosomes are the potential signal for ribosome dysfunction, leading to accelerated turnover of the ribosome itself. | ||||||||||||
| 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 | 7zw0.cif.gz | 4.6 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7zw0.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 7zw0.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zw/7zw0 ftp://data.pdbj.org/pub/pdb/validation_reports/zw/7zw0 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 14990MC M: map data used to model this data 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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Components
-RNA chain , 6 types, 7 molecules LA2smslsnLCLD
| #1: RNA chain | Mass: 1097493.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() | ||||
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| #3: RNA chain | Mass: 579761.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() | ||||
| #39: RNA chain | Mass: 9439.882 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() | ||||
| #40: RNA chain | Mass: 24502.477 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #41: RNA chain | | Mass: 38951.105 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #42: RNA chain | | Mass: 50682.922 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+60S ribosomal protein ... , 42 types, 43 molecules LBLELFLGLHLILJLKLLLMLNLOLPLQLRLSLTLULVLWLXLYLZLaLbLcLdLeLfLg...
+40S ribosomal protein ... , 30 types, 30 molecules sPsQsRsAsSsBsTsUsVsWsCsXsDsYsZsFsGsHsIsJsasbscsdsKsesfsgsNsL
-Protein , 6 types, 6 molecules sEsMsOsjsksh
| #6: Protein | Mass: 16031.907 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #32: Protein | Mass: 6675.723 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #35: Protein | Mass: 34841.219 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #37: Protein | Mass: 27164.072 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #38: Protein | Mass: 12169.823 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #84: Protein | Mass: 108662.328 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 3 types, 359 molecules 




| #85: Chemical | ChemComp-MG / #86: Chemical | ChemComp-SPD / | #87: Chemical | ChemComp-ZN / |
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-Details
| Has ligand of interest | N |
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-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: Fap1-Yil161w-Fpr1-bound yeast 80S ribosome in rotated state Type: RIBOSOME / Entity ID: #1-#84 / Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| 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: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 500 nm |
| Image recording | Electron dose: 43.4 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 2.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 114964 / Symmetry type: POINT |
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About Yorodumi






Germany, European Union, 3items
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FIELD EMISSION GUN