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Open data
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Basic information
| Entry | Database: PDB / ID: 9g8p | ||||||||||||||||||
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| Title | 40S-bound human SKI2-exosome complex | ||||||||||||||||||
Components |
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Keywords | RIBOSOME / RNA-binding / RNA-degradation / cytoplasm / helicase | ||||||||||||||||||
| Function / homology | Function and homology informationDNA deamination / nucleolar exosome (RNase complex) / exoribonuclease II activity / exoribonuclease II / Dom34-Hbs1 complex / nuclear-transcribed mRNA catabolic process, no-go decay / CUT catabolic process / Ski complex / cytoplasmic exosome (RNase complex) / U1 snRNA 3'-end processing ...DNA deamination / nucleolar exosome (RNase complex) / exoribonuclease II activity / exoribonuclease II / Dom34-Hbs1 complex / nuclear-transcribed mRNA catabolic process, no-go decay / CUT catabolic process / Ski complex / cytoplasmic exosome (RNase complex) / U1 snRNA 3'-end processing / U5 snRNA 3'-end processing / TRAMP-dependent tRNA surveillance pathway / mRNA decay by 3' to 5' exoribonuclease / exosome (RNase complex) / U4 snRNA 3'-end processing / nuclear polyadenylation-dependent rRNA catabolic process / poly(A)-dependent snoRNA 3'-end processing / nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay / nuclear exosome (RNase complex) / exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / ATF4 activates genes in response to endoplasmic reticulum stress / Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / 3'-5' RNA helicase activity / positive regulation of isotype switching / histone mRNA catabolic process / nuclear mRNA surveillance / rRNA catabolic process / 7S RNA binding / mRNA 3'-UTR AU-rich region binding / isotype switching / ribosome disassembly / RNA catabolic process / KSRP (KHSRP) binds and destabilizes mRNA / maturation of 5.8S rRNA / nuclear chromosome / mRNA catabolic process / Association of TriC/CCT with target proteins during biosynthesis / nuclear-transcribed mRNA catabolic process / translation elongation factor activity / Major pathway of rRNA processing in the nucleolus and cytosol / RNA processing / cytosolic ribosome / rescue of stalled cytosolic ribosome / euchromatin / fibrillar center / rRNA processing / regulation of translation / chromosome / positive regulation of cell growth / 3'-5'-RNA exonuclease activity / defense response to virus / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / RNA polymerase II-specific DNA-binding transcription factor binding / RNA helicase activity / immune response / ciliary basal body / RNA helicase / translation / intracellular membrane-bounded organelle / GTPase activity / centrosome / GTP binding / nucleolus / enzyme binding / signal transduction / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / RNA binding / extracellular exosome / nucleoplasm / ATP binding / identical protein binding / nucleus / membrane / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||||||||||||||
| Biological species | Homo sapiens (human) Cricket paralysis virus | ||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 7 Å | ||||||||||||||||||
Authors | Koegel, A. / Keidel, A. / Loukeri, M.J. / Kuhn, C.C. / Langer, L.M. / Schaefer, I.B. / Conti, E. | ||||||||||||||||||
| Funding support | Germany, European Union, Denmark, 5items
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Citation | Journal: Nature / Year: 2024Title: Structural basis of mRNA decay by the human exosome-ribosome supercomplex. Authors: Alexander Kögel / Achim Keidel / Matina-Jasemi Loukeri / Christopher C Kuhn / Lukas M Langer / Ingmar B Schäfer / Elena Conti / ![]() Abstract: The interplay between translation and mRNA decay is widespread in human cells. In quality-control pathways, exonucleolytic degradation of mRNA associated with translating ribosomes is mediated ...The interplay between translation and mRNA decay is widespread in human cells. In quality-control pathways, exonucleolytic degradation of mRNA associated with translating ribosomes is mediated largely by the cytoplasmic exosome, which includes the exoribonuclease complex EXO10 and the helicase complex SKI238 (refs. ). The helicase can extract mRNA from the ribosome and is expected to transfer it to the exoribonuclease core through a bridging factor, HBS1L3 (also known as SKI7), but the mechanisms of this molecular handover remain unclear. Here we reveal how human EXO10 is recruited by HBS1L3 (SKI7) to an active ribosome-bound SKI238 complex. We show that rather than a sequential handover, a direct physical coupling mechanism takes place, which culminates in the formation of a cytoplasmic exosome-ribosome supercomplex. Capturing the structure during active decay reveals a continuous path in which an RNA substrate threads from the 80S ribosome through the SKI2 helicase into the exoribonuclease active site of the cytoplasmic exosome complex. The SKI3 subunit of the complex directly binds to HBS1L3 (SKI7) and also engages a surface of the 40S subunit, establishing a recognition platform in collided disomes. Exosome and ribosome thus work together as a single structural and functional unit in co-translational mRNA decay, coordinating their activities in a transient supercomplex. | ||||||||||||||||||
| 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 | 9g8p.cif.gz | 789.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9g8p.ent.gz | 630.5 KB | Display | PDB format |
| PDBx/mmJSON format | 9g8p.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9g8p_validation.pdf.gz | 1.5 MB | Display | wwPDB validaton report |
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| Full document | 9g8p_full_validation.pdf.gz | 1.5 MB | Display | |
| Data in XML | 9g8p_validation.xml.gz | 143.5 KB | Display | |
| Data in CIF | 9g8p_validation.cif.gz | 217.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g8/9g8p ftp://data.pdbj.org/pub/pdb/validation_reports/g8/9g8p | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 51135MC ![]() 9g8mC ![]() 9g8nC ![]() 9g8oC ![]() 9g8qC ![]() 9g8rC 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
-Exosome complex component ... , 9 types, 9 molecules NOFHJGIKL
| #1: Protein | Mass: 30429.893 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: EXOSC8, OIP2, RRP43 / Production host: ![]() |
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| #2: Protein | Mass: 25636.312 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: EXOSC5, CML28, RRP46 / Production host: ![]() |
| #3: Protein | Mass: 32216.762 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: EXOSC7, KIAA0116, RRP42 / Production host: ![]() |
| #4: Protein | Mass: 29940.502 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: EXOSC3, RRP40, CGI-102 / Production host: ![]() |
| #5: Protein | Mass: 21835.100 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: EXOSC1, CSL4, CGI-108 / Production host: ![]() |
| #8: Protein | Mass: 28267.127 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: EXOSC6, MTR3 / Production host: ![]() |
| #9: Protein | Mass: 33190.355 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: EXOSC2, RRP4 / Production host: ![]() |
| #11: Protein | Mass: 49370.312 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: EXOSC9, PMSCL1 / Production host: ![]() |
| #13: Protein | Mass: 26416.996 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: EXOSC4, RRP41, SKI6 / Production host: ![]() |
-RNA chain , 1 types, 1 molecules X
| #6: RNA chain | Mass: 13422.399 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Cricket paralysis virus |
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-Protein , 3 types, 3 molecules AEM
| #7: Protein | Mass: 137913.688 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SKIV2L, DDX13, SKI2W, SKIV2, W / Production host: ![]() References: UniProt: Q15477, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement |
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| #10: Protein | Mass: 30196.131 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HBS1L, HBS1, KIAA1038 / Production host: ![]() References: UniProt: Q9Y450, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement |
| #12: Protein | Mass: 121108.555 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DIS3L, DIS3L1, KIAA1955 / Production host: ![]() |
-Details
| Has protein modification | 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: 40S-bound human SKI2-exosome complex / Type: RIBOSOME / Entity ID: #13, #1-#12 / Source: RECOMBINANT |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.4 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R2/1 |
| Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2400 nm / Nominal defocus min: 600 nm |
| Image recording | Electron dose: 64.2 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.19.2_4158: / Category: model refinement |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| 3D reconstruction | Resolution: 7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 12714 / Symmetry type: POINT |
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About Yorodumi




Homo sapiens (human)
Cricket paralysis virus
Germany, European Union,
Denmark, 5items
Citation











PDBj











































FIELD EMISSION GUN