[English] 日本語
Yorodumi- PDB-6q8y: Cryo-EM structure of the mRNA translating and degrading yeast 80S... -
+
Open data
-
Basic information
| Entry | Database: PDB / ID: 6q8y | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Title | Cryo-EM structure of the mRNA translating and degrading yeast 80S ribosome-Xrn1 nuclease complex | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Keywords | TRANSLATION / ribosome / stalling / nuclease / exoribonuclease / Xrn1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationnuclear-transcribed mRNA catabolic process, 5'-3' exonucleolytic nonsense-mediated decay / eisosome membrane domain/MCC / sno(s)RNA processing / nuclear-transcribed mRNA catabolic process, no-go decay / NAD-cap decapping / eukaryotic initiation factor 4G binding / karyogamy / tRNA decay / 5'-3' RNA exonuclease activity / traversing start control point of mitotic cell cycle ...nuclear-transcribed mRNA catabolic process, 5'-3' exonucleolytic nonsense-mediated decay / eisosome membrane domain/MCC / sno(s)RNA processing / nuclear-transcribed mRNA catabolic process, no-go decay / NAD-cap decapping / eukaryotic initiation factor 4G binding / karyogamy / tRNA decay / 5'-3' RNA exonuclease activity / traversing start control point of mitotic cell cycle / rRNA catabolic process / 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 / cellular response to nitrogen starvation / ribosome-associated ubiquitin-dependent protein catabolic process / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / regulation of telomere maintenance / 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 / negative regulation of macroautophagy / Major pathway of rRNA processing in the nucleolus and cytosol / mRNA destabilization / 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) / positive regulation of protein kinase activity / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / nuclear-transcribed mRNA catabolic process / negative regulation of translational frameshifting / L13a-mediated translational silencing of Ceruloplasmin expression / translational elongation / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / G-protein alpha-subunit binding / ribosomal large subunit export from nucleus / positive regulation of transcription initiation by RNA polymerase II / 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 regulator activity / ribosomal small subunit export from nucleus / DNA-(apurinic or apyrimidinic site) endonuclease activity / rescue of stalled cytosolic ribosome / 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 / P-body / positive regulation of transcription elongation by RNA polymerase II / 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 / Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters / cytosolic large ribosomal subunit / microtubule / cytoplasmic translation / negative regulation of translation / rRNA binding / protein ubiquitination / structural constituent of ribosome Similarity search - Function | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Authors | Tesina, P. / Heckel, E. / Cheng, J. / Buschauer, R. / Kater, L. / Berninghausen, O. / Becker, T. / Beckmann, R. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Funding support | Germany, 2items
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Citation | Journal: Nat Struct Mol Biol / Year: 2019Title: Structure of the 80S ribosome-Xrn1 nuclease complex. Authors: Petr Tesina / Elisabeth Heckel / Jingdong Cheng / Micheline Fromont-Racine / Robert Buschauer / Lukas Kater / Birgitta Beatrix / Otto Berninghausen / Alain Jacquier / Thomas Becker / Roland Beckmann / ![]() Abstract: Messenger RNA (mRNA) homeostasis represents an essential part of gene expression, in which the generation of mRNA by RNA polymerase is counter-balanced by its degradation by nucleases. The conserved ...Messenger RNA (mRNA) homeostasis represents an essential part of gene expression, in which the generation of mRNA by RNA polymerase is counter-balanced by its degradation by nucleases. The conserved 5'-to-3' exoribonuclease Xrn1 has a crucial role in eukaryotic mRNA homeostasis by degrading decapped or cleaved mRNAs post-translationally and, more surprisingly, also co-translationally. Here we report that active Xrn1 can directly and specifically interact with the translation machinery. A cryo-electron microscopy structure of a programmed Saccharomyces cerevisiae 80S ribosome-Xrn1 nuclease complex reveals how the conserved core of Xrn1 enables binding at the mRNA exit site of the ribosome. This interface provides a conduit for channelling of the mRNA from the ribosomal decoding site directly into the active center of the nuclease, thus separating mRNA decoding from degradation by only 17 ± 1 nucleotides. These findings explain how rapid 5'-to-3' mRNA degradation is coupled efficiently to its final round of mRNA translation. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| History |
|
-
Structure visualization
| Movie |
Movie viewer |
|---|---|
| Structure viewer | Molecule: Molmil Jmol/JSmol |
-
Downloads & links
-
Download
| PDBx/mmCIF format | 6q8y.cif.gz | 4.5 MB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb6q8y.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 6q8y.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q8/6q8y ftp://data.pdbj.org/pub/pdb/validation_reports/q8/6q8y | HTTPS FTP |
|---|
-Related structure data
| Related structure data | ![]() 4474MC M: map data used to model this data C: citing same article ( |
|---|---|
| Similar structure data |
-
Links
-
Assembly
| Deposited unit | ![]()
|
|---|---|
| 1 |
|
-
Components
-RNA chain , 7 types, 7 molecules 2lnmBQBRBS
| #1: RNA chain | Mass: 578836.375 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
|---|---|
| #34: RNA chain | Mass: 5490.350 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() |
| #35: RNA chain | Mass: 24468.551 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #36: RNA chain | Mass: 24004.262 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #54: RNA chain | Mass: 1097493.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #55: RNA chain | Mass: 38951.105 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #56: RNA chain | Mass: 50682.922 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+60S ribosomal protein ... , 40 types, 40 molecules AAABACADAEAFAGAHAIAJAKALAMANAPAQARASATAUAVAWAXAYBABBBCBDBEBF...
-Protein , 5 types, 5 molecules AOzBNO
| #16: Protein | Mass: 6032.321 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
|---|---|
| #33: Protein | Mass: 107653.734 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P22147, Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters |
| #58: Protein | Mass: 22908.338 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #69: Protein | Mass: 5704.610 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #70: Protein | Mass: 34710.023 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+40S ribosomal protein ... , 30 types, 30 molecules abcdefgACDEFGHJKLMPQRSTUVWXYZI
-Non-polymers , 2 types, 10 molecules 


| #83: Chemical | ChemComp-ZN / #84: Chemical | |
|---|
-Details
| Has protein modification | Y |
|---|
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
|---|---|
| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
| Component |
| ||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Source (natural) |
| ||||||||||||||||||||||||||||||||||||||||||
| Source (recombinant) | Organism: ![]() | ||||||||||||||||||||||||||||||||||||||||||
| Buffer solution | pH: 7.5 | ||||||||||||||||||||||||||||||||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||||||||||||||
| Vitrification | Cryogen name: ETHANE |
-
Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
|---|---|
| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD |
| Image recording | Electron dose: 2.5 e/Å2 / Film or detector model: FEI FALCON II (4k x 4k) |
-
Processing
| Software | Name: PHENIX / Version: 1.14_3260: / Classification: refinement |
|---|---|
| EM software | Name: PHENIX / Category: model refinement |
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| 3D reconstruction | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 217000 / Symmetry type: POINT |
Movie
Controller
About Yorodumi





Germany, 2items
Citation
UCSF Chimera










PDBj

































