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Yorodumi- PDB-8q7q: Structure of the recycling U5 snRNP bound to chaperones CD2BP2 an... -
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Basic information
| Entry | Database: PDB / ID: 8q7q | |||||||||
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| Title | Structure of the recycling U5 snRNP bound to chaperones CD2BP2 and TSSC4 (State 2) | |||||||||
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Keywords | SPLICING / U5 snRNP / CD2BP2 / TSSC4 / spliceosome | |||||||||
| Function / homology | Function and homology informationRNA localization / U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / U7 snRNP / cis assembly of pre-catalytic spliceosome / histone pre-mRNA 3'end processing complex / nuclear histone mRNA catabolic process / SLBP independent Processing of Histone Pre-mRNAs / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs ...RNA localization / U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / U7 snRNP / cis assembly of pre-catalytic spliceosome / histone pre-mRNA 3'end processing complex / nuclear histone mRNA catabolic process / SLBP independent Processing of Histone Pre-mRNAs / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs / 7-methylguanosine cap hypermethylation / U12-type spliceosomal complex / U1 snRNP binding / pICln-Sm protein complex / U2-type catalytic step 1 spliceosome / methylosome / RNA splicing, via transesterification reactions / sno(s)RNA-containing ribonucleoprotein complex / small nuclear ribonucleoprotein complex / SMN-Sm protein complex / spliceosomal tri-snRNP complex / commitment complex / P granule / U4 snRNP / snRNP binding / U2-type precatalytic spliceosome / U2-type prespliceosome assembly / U2-type catalytic step 2 spliceosome / U2-type spliceosomal complex / telomerase holoenzyme complex / telomerase RNA binding / U1 snRNP / U2 snRNP / spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) / RNA Polymerase II Transcription Termination / protein methylation / U2-type prespliceosome / K63-linked polyubiquitin modification-dependent protein binding / precatalytic spliceosome / mRNA Splicing - Minor Pathway / spliceosomal complex assembly / negative regulation of mRNA splicing, via spliceosome / spliceosomal tri-snRNP complex assembly / U5 snRNP / U5 snRNA binding / pre-mRNA intronic binding / molecular sequestering activity / U2 snRNA binding / U6 snRNA binding / U4/U6 x U5 tri-snRNP complex / ribonucleoprotein complex binding / Cajal body / U1 snRNA binding / RNA processing / spliceosomal snRNP assembly / catalytic step 2 spliceosome / spliceosomal complex / mRNA Splicing - Major Pathway / RNA splicing / helicase activity / cellular response to xenobiotic stimulus / cellular response to tumor necrosis factor / response to cocaine / mRNA splicing, via spliceosome / osteoblast differentiation / mRNA processing / mRNA Polyadenylation / cellular response to lipopolysaccharide / Dengue Virus-Host Interactions / snRNP Assembly / SARS-CoV-2 modulates host translation machinery / nuclear body / protein-macromolecule adaptor activity / RNA helicase activity / nuclear speck / RNA helicase / GTPase activity / GTP binding / protein-containing complex binding / enzyme binding / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / RNA binding / extracellular exosome / nucleoplasm / ATP binding / membrane / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||
Authors | Riabov Bassat, D. / Plaschka, C. / Vorlaender, M.K. | |||||||||
| Funding support | European Union, 2items
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Citation | Journal: Nat Struct Mol Biol / Year: 2024Title: Structural basis of human U5 snRNP late biogenesis and recycling. Authors: Daria Riabov Bassat / Supapat Visanpattanasin / Matthias K Vorländer / Laura Fin / Alexander W Phillips / Clemens Plaschka / ![]() Abstract: Pre-mRNA splicing by the spliceosome requires the biogenesis and recycling of its small nuclear ribonucleoprotein (snRNP) complexes, which are consumed in each round of splicing. The human U5 snRNP ...Pre-mRNA splicing by the spliceosome requires the biogenesis and recycling of its small nuclear ribonucleoprotein (snRNP) complexes, which are consumed in each round of splicing. The human U5 snRNP is the ~1 MDa 'heart' of the spliceosome and is recycled through an unknown mechanism involving major architectural rearrangements and the dedicated chaperones CD2BP2 and TSSC4. Late steps in U5 snRNP biogenesis similarly involve these chaperones. Here we report cryo-electron microscopy structures of four human U5 snRNP-CD2BP2-TSSC4 complexes, revealing how a series of molecular events primes the U5 snRNP to generate the ~2 MDa U4/U6.U5 tri-snRNP, the largest building block of the spliceosome. | |||||||||
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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 | 8q7q.cif.gz | 1.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8q7q.ent.gz | 1 MB | Display | PDB format |
| PDBx/mmJSON format | 8q7q.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q7/8q7q ftp://data.pdbj.org/pub/pdb/validation_reports/q7/8q7q | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 18229MC ![]() 8q7vC ![]() 8q7wC ![]() 8q7xC 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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Components
-RNA chain , 1 types, 1 molecules 5
| #1: RNA chain | Mass: 37254.855 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
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-Protein , 6 types, 6 molecules ACFGHb
| #2: Protein | Mass: 273974.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: k562 / References: UniProt: Q6P2Q9 |
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| #4: Protein | Mass: 109560.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q15029 |
| #6: Protein | Mass: 107092.242 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O94906 |
| #7: Protein | Mass: 37841.523 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: the N-terminal GP comes from a cleaved 3C tag / Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): K562 cells / Production host: Homo sapiens (human) / References: UniProt: O95400 |
| #8: Protein | Mass: 34366.465 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y5U2 |
| #10: Protein | Mass: 24642.131 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P14678 |
-U5 small nuclear ribonucleoprotein ... , 2 types, 2 molecules BD
| #3: Protein | Mass: 244823.422 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O75643, RNA helicase |
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| #5: Protein | Mass: 39359.492 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96DI7 |
-Small nuclear ribonucleoprotein ... , 6 types, 6 molecules acdefg
| #9: Protein | Mass: 13310.653 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62314 |
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| #11: Protein | Mass: 13551.928 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62316 |
| #12: Protein | Mass: 13940.308 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62318 |
| #13: Protein | Mass: 10817.601 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62304 |
| #14: Protein | Mass: 9734.171 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62306 |
| #15: Protein | Mass: 8508.084 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62308 |
-Non-polymers , 2 types, 2 molecules 


| #16: Chemical | ChemComp-MG / |
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| #17: Chemical | ChemComp-GTP / |
-Details
| Has ligand of interest | Y |
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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: Structure of the recycling U5 snRNP bound to chaperones CD2BP2 and TSSC4 (State , Map 2) Type: COMPLEX / Entity ID: #1-#15 / Source: NATURAL |
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| Molecular weight | Value: 1 MDa / Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.9 |
| 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: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 500 nm |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 19393 / Symmetry type: POINT |
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