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Open data
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Basic information
| Entry | Database: PDB / ID: 7a5p | |||||||||
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| Title | Human C Complex Spliceosome - Medium-resolution PERIPHERY | |||||||||
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Keywords | SPLICING / human C complex / spliceosome / hC / human step 1 spliceosome | |||||||||
| Function / homology | Function and homology informationstriated muscle dense body / exon-exon junction subcomplex mago-y14 / negative regulation of selenocysteine incorporation / cellular response to selenite ion / exon-exon junction complex / regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / regulation of vitamin D receptor signaling pathway / selenocysteine insertion sequence binding / mRNA metabolic process / regulation of translation at postsynapse, modulating synaptic transmission ...striated muscle dense body / exon-exon junction subcomplex mago-y14 / negative regulation of selenocysteine incorporation / cellular response to selenite ion / exon-exon junction complex / regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / regulation of vitamin D receptor signaling pathway / selenocysteine insertion sequence binding / mRNA metabolic process / regulation of translation at postsynapse, modulating synaptic transmission / regulation of retinoic acid receptor signaling pathway / U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / U7 snRNP / generation of catalytic spliceosome for first transesterification step / Z-decay: degradation of maternal mRNAs by zygotically expressed factors / 3'-5' RNA helicase activity / cis assembly of pre-catalytic spliceosome / histone pre-mRNA 3'end processing complex / nuclear histone mRNA catabolic process / embryonic cranial skeleton morphogenesis / U4atac snRNP / U4atac/U6atac snRNP / SLBP independent Processing of Histone Pre-mRNAs / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs / regulation of mRNA processing / Deadenylation of mRNA / C2H2 zinc finger domain binding / U11/U12 snRNP / negative regulation of excitatory postsynaptic potential / poly(A) binding / U4atac/U6atac x U5 tri-snRNP complex / embryonic brain development / 7-methylguanosine cap hypermethylation / U12-type spliceosomal complex / nuclear retinoic acid receptor binding / U1 snRNP binding / regulation of mRNA splicing, via spliceosome / post-spliceosomal complex / positive regulation of mRNA splicing, via spliceosome / RNA splicing, via transesterification reactions / pICln-Sm protein complex / snRNP binding / mRNA 3'-end processing / methylosome / U12-type catalytic step 2 spliceosome / post-mRNA release spliceosomal complex / muscle organ development / small nuclear ribonucleoprotein complex / SMN-Sm protein complex / U12-type precatalytic spliceosome / spliceosomal tri-snRNP complex / M-decay: degradation of maternal mRNAs by maternally stored factors / positive regulation of vitamin D receptor signaling pathway / RNA Polymerase II Transcription Termination / commitment complex / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / P granule / host-mediated activation of viral transcription / U2-type precatalytic spliceosome / Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells / RUNX3 regulates NOTCH signaling / Notch binding / U2-type spliceosomal complex / nuclear vitamin D receptor binding / telomerase holoenzyme complex / U2-type prespliceosome assembly / Transport of Mature mRNA derived from an Intron-Containing Transcript / NOTCH4 Intracellular Domain Regulates Transcription / telomerase RNA binding / pre-mRNA binding / U4/U6 snRNP / U2-type catalytic step 2 spliceosome / positive regulation of neurogenesis / spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) / U1 snRNP / U2 snRNP / NOTCH3 Intracellular Domain Regulates Transcription / U2-type catalytic step 1 spliceosome / protein methylation / exploration behavior / U4 snRNP / mRNA stabilization / U2-type prespliceosome / mRNA cis splicing, via spliceosome / nuclear androgen receptor binding / cyclosporin A binding / K63-linked polyubiquitin modification-dependent protein binding / generation of catalytic spliceosome for second transesterification step / ubiquitin-ubiquitin ligase activity / Notch-HLH transcription pathway / Formation of paraxial mesoderm / regulation of alternative mRNA splicing, via spliceosome / precatalytic spliceosome / positive regulation of transforming growth factor beta receptor signaling pathway / WD40-repeat domain binding / negative regulation of DNA damage response, signal transduction by p53 class mediator / mRNA 3'-splice site recognition / SMAD binding Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 5 Å | |||||||||
Authors | Bertram, K. / Kastner, B. | |||||||||
| Funding support | Germany, 2items
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Citation | Journal: Mol Cell / Year: 2020Title: Structural Insights into the Roles of Metazoan-Specific Splicing Factors in the Human Step 1 Spliceosome. Authors: Karl Bertram / Leyla El Ayoubi / Olexandr Dybkov / Dmitry E Agafonov / Cindy L Will / Klaus Hartmuth / Henning Urlaub / Berthold Kastner / Holger Stark / Reinhard Lührmann / ![]() Abstract: Human spliceosomes contain numerous proteins absent in yeast, whose functions remain largely unknown. Here we report a 3D cryo-EM structure of the human spliceosomal C complex at 3.4 Å core ...Human spliceosomes contain numerous proteins absent in yeast, whose functions remain largely unknown. Here we report a 3D cryo-EM structure of the human spliceosomal C complex at 3.4 Å core resolution and 4.5-5.7 Å at its periphery, and aided by protein crosslinking we determine its molecular architecture. Our structure provides additional insights into the spliceosome's architecture between the catalytic steps of splicing, and how proteins aid formation of the spliceosome's catalytically active RNP (ribonucleoprotein) conformation. It reveals the spatial organization of the metazoan-specific proteins PPWD1, WDR70, FRG1, and CIR1 in human C complexes, indicating they stabilize functionally important protein domains and RNA structures rearranged/repositioned during the B to C transition. Structural comparisons with human B, C, and P complexes reveal an intricate cascade of RNP rearrangements during splicing catalysis, with intermediate RNP conformations not found in yeast, and additionally elucidate the structural basis for the sequential recruitment of metazoan-specific spliceosomal proteins. | |||||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7a5p.cif.gz | 1.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7a5p.ent.gz | 1.1 MB | Display | PDB format |
| PDBx/mmJSON format | 7a5p.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a5/7a5p ftp://data.pdbj.org/pub/pdb/validation_reports/a5/7a5p | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 11570MC ![]() 6zymC C: citing same article ( M: map data used to model this data |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-RNA chain , 4 types, 4 molecules 256Y
| #1: RNA chain | Mass: 312349.656 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 36516 |
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| #2: RNA chain | Mass: 36908.668 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 36515 |
| #3: RNA chain | Mass: 34098.270 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Strain: HeLa S3 |
| #20: RNA chain | Mass: 103979.148 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Strain: HeLa S3 |
-Protein , 17 types, 18 molecules 8ACLOSUbmopquvwxyz
| #4: Protein | Mass: 17379.371 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Strain: HeLa S3 | ||||||||||||||||||
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| #5: Protein | Mass: 273974.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q6P2Q9 | ||||||||||||||||||
| #6: Protein | Mass: 61610.703 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q13573 | ||||||||||||||||||
| #10: Protein | Mass: 92406.883 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q99459 | ||||||||||||||||||
| #13: Protein | Mass: 100610.008 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BZJ0 | ||||||||||||||||||
| #15: Protein | Mass: 300255.312 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9UQ35 | ||||||||||||||||||
| #17: Protein | Mass: 173331.328 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O60306, RNA helicase | ||||||||||||||||||
| #22: Protein | Mass: 24642.131 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P14678#28: Protein | | Mass: 33475.773 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9UNP9, peptidylprolyl isomerase#29: Protein | | Mass: 73306.172 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9NW82#30: 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#33: Protein | | Mass: 37141.816 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BW85#34: Protein | | Mass: 17189.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P61326#35: Protein | | Mass: 19925.070 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y5S9#36: Protein | | Mass: 29227.492 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q14331#37: Protein | | Mass: 46930.961 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P38919, RNA helicase#38: Protein | | Mass: 73679.891 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96BP3, peptidylprolyl isomerase |
-Pre-mRNA-processing factor ... , 2 types, 5 molecules EGHIJ
| #7: Protein | Mass: 65612.180 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O60508 |
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| #8: Protein | Mass: 55245.547 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: Q9UMS4, RING-type E3 ubiquitin transferase |
-Pre-mRNA-splicing factor ... , 7 types, 7 molecules KMNPTrs
| #9: Protein | Mass: 26163.420 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O75934 |
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| #11: Protein | Mass: 100148.711 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9HCS7 |
| #12: Protein | Mass: 28780.518 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95926 |
| #14: Protein | Mass: 46959.555 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9NW64 |
| #16: Protein | Mass: 105646.578 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9HCG8 |
| #31: Protein | Mass: 140777.688 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q92620, RNA helicase |
| #32: Protein | Mass: 33046.254 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9ULR0 |
-U2 small nuclear ribonucleoprotein ... , 2 types, 2 molecules WX
| #18: Protein | Mass: 28484.592 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P09661 |
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| #19: Protein | Mass: 25524.367 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P08579 |
-Small nuclear ribonucleoprotein ... , 6 types, 12 molecules alcndhejfigk
| #21: Protein | Mass: 13940.308 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62318#23: Protein | Mass: 13310.653 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62314#24: Protein | Mass: 13551.928 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62316#25: Protein | Mass: 10817.601 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62304#26: Protein | Mass: 9734.171 Da / Num. of mol.: 2 / Source method: isolated from a natural source Details: MSLPLNPKPFLNGLTGKPVMVKLKWGMEYKGYLVSVDGYMNMQLANTEEYIDGALSGHLGEVLIRCNNVLYIRGVEEEEEDGEMRE Source: (natural) Homo sapiens (human) / References: UniProt: P62306#27: Protein | Mass: 8508.084 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62308 |
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-Details
| Has protein modification | 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: Human C Complex Spliceosome / Type: RIBOSOME / Entity ID: all / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) / Strain: HeLa S3 |
| Buffer solution | pH: 7.9 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE / Humidity: 100 % |
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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 |
| Image recording | Electron dose: 6 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 5 Å / Resolution method: OTHER / Num. of particles: 69000 / Symmetry type: POINT |
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About Yorodumi




Homo sapiens (human)
Germany, 2items
Citation
UCSF Chimera











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