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Open data
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Basic information
| Entry | Database: PDB / ID: 6qdv | ||||||||||||
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| Title | Human post-catalytic P complex spliceosome | ||||||||||||
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Keywords | SPLICING / spliceosome / RNA / complex | ||||||||||||
| Function / homology | Function and homology informationsecond spliceosomal transesterification activity / exon-exon junction subcomplex mago-y14 / negative regulation of selenocysteine incorporation / regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / cellular response to selenite ion / selenocysteine insertion sequence binding / exon-exon junction complex / pre-mRNA 3'-splice site binding / regulation of translation at postsynapse, modulating synaptic transmission / regulation of retinoic acid receptor signaling pathway ...second spliceosomal transesterification activity / exon-exon junction subcomplex mago-y14 / negative regulation of selenocysteine incorporation / regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / cellular response to selenite ion / selenocysteine insertion sequence binding / exon-exon junction complex / pre-mRNA 3'-splice site binding / regulation of translation at postsynapse, modulating synaptic transmission / regulation of retinoic acid receptor signaling pathway / granulocyte differentiation / post-mRNA release spliceosomal complex / renal system process / U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / 3'-5' RNA helicase activity / endonucleolytic cleavage of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / U7 snRNP / negative regulation of toll-like receptor signaling pathway / generation of catalytic spliceosome for first transesterification step / Z-decay: degradation of maternal mRNAs by zygotically expressed factors / histone pre-mRNA 3'end processing complex / cis assembly of pre-catalytic spliceosome / regulation of mRNA processing / regulation of vitamin D receptor signaling pathway / negative regulation of excitatory postsynaptic potential / negative regulation of interleukin-8 production / SLBP independent Processing of Histone Pre-mRNAs / negative regulation of lipopolysaccharide-mediated signaling pathway / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs / Deadenylation of mRNA / spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) / nuclear retinoic acid receptor binding / embryonic brain development / protein methylation / embryonic cranial skeleton morphogenesis / oocyte development / U12-type spliceosomal complex / alternative mRNA splicing, via spliceosome / poly(A) binding / 7-methylguanosine cap hypermethylation / negative regulation of interferon-beta production / U1 snRNP binding / sno(s)RNA-containing ribonucleoprotein complex / methylosome / mRNA 3'-end processing / M-decay: degradation of maternal mRNAs by maternally stored factors / RNA splicing, via transesterification reactions / ATP-dependent activity, acting on RNA / pICln-Sm protein complex / C2H2 zinc finger domain binding / U2-type catalytic step 1 spliceosome / pre-mRNA binding / regulation of mRNA splicing, via spliceosome / snRNP binding / positive regulation of mRNA splicing, via spliceosome / small nuclear ribonucleoprotein complex / SMN-Sm protein complex / spliceosomal tri-snRNP complex / host-mediated activation of viral transcription / P granule / telomerase holoenzyme complex / U2-type precatalytic spliceosome / positive regulation of vitamin D receptor signaling pathway / commitment complex / mRNA cis splicing, via spliceosome / telomerase RNA binding / U2-type spliceosomal complex / nuclear vitamin D receptor binding / U2-type prespliceosome assembly / Notch binding / Transport of Mature mRNA derived from an Intron-Containing Transcript / positive regulation of alpha-beta T cell differentiation / U2-type catalytic step 2 spliceosome / Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells / RUNX3 regulates NOTCH signaling / positive regulation of neurogenesis / NOTCH4 Intracellular Domain Regulates Transcription / U4 snRNP / RNA Polymerase II Transcription Termination / U2 snRNP / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / U1 snRNP / NOTCH3 Intracellular Domain Regulates Transcription / negative regulation of type I interferon-mediated signaling pathway / U2-type prespliceosome / inner cell mass cell proliferation / WD40-repeat domain binding / ubiquitin-ubiquitin ligase activity / protein peptidyl-prolyl isomerization / K63-linked polyubiquitin modification-dependent protein binding / snoRNA binding / nuclear androgen receptor binding / precatalytic spliceosome / negative regulation of NF-kappaB transcription factor activity / regulation of alternative mRNA splicing, via spliceosome / lipid biosynthetic process / Notch-HLH transcription pathway / hematopoietic stem cell proliferation Similarity search - Function | ||||||||||||
| Biological species | Homo sapiens (human)![]() Human adenovirus 2 | ||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | ||||||||||||
Authors | Fica, S.M. / Oubridge, C. / Wilkinson, M.E. / Newman, A.J. / Nagai, K. | ||||||||||||
| Funding support | United Kingdom, 2items
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Citation | Journal: Science / Year: 2019Title: A human postcatalytic spliceosome structure reveals essential roles of metazoan factors for exon ligation. Authors: Sebastian M Fica / Chris Oubridge / Max E Wilkinson / Andrew J Newman / Kiyoshi Nagai / ![]() Abstract: During exon ligation, the spliceosome recognizes the 3'-splice site (3'SS) of precursor messenger RNA (pre-mRNA) through non-Watson-Crick pairing with the 5'SS and the branch adenosine, in a ...During exon ligation, the spliceosome recognizes the 3'-splice site (3'SS) of precursor messenger RNA (pre-mRNA) through non-Watson-Crick pairing with the 5'SS and the branch adenosine, in a conformation stabilized by Prp18 and Prp8. Here we present the 3.3-angstrom cryo-electron microscopy structure of a human postcatalytic spliceosome just after exon ligation. The 3'SS docks at the active site through conserved RNA interactions in the absence of Prp18. Unexpectedly, the metazoan-specific FAM32A directly bridges the 5'-exon and intron 3'SS of pre-mRNA and promotes exon ligation, as shown by functional assays. CACTIN, SDE2, and NKAP-factors implicated in alternative splicing-further stabilize the catalytic conformation of the spliceosome during exon ligation. Together these four proteins act as exon ligation factors. Our study reveals how the human spliceosome has co-opted additional proteins to modulate a conserved RNA-based mechanism for 3'SS selection and to potentially fine-tune alternative splicing at the exon ligation stage. | ||||||||||||
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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 | 6qdv.cif.gz | 2.7 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb6qdv.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 6qdv.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6qdv_validation.pdf.gz | 1.8 MB | Display | wwPDB validaton report |
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| Full document | 6qdv_full_validation.pdf.gz | 1.8 MB | Display | |
| Data in XML | 6qdv_validation.xml.gz | 318.6 KB | Display | |
| Data in CIF | 6qdv_validation.cif.gz | 539.7 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qd/6qdv ftp://data.pdbj.org/pub/pdb/validation_reports/qd/6qdv | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 4525MC ![]() 4526C ![]() 4527C ![]() 4528C ![]() 4529C ![]() 4530C ![]() 4532C ![]() 4533C ![]() 4534C ![]() 4535C M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Assembly
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Components
-RNA chain , 5 types, 5 molecules 256EI
| #1: RNA chain | Mass: 60459.621 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
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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) |
| #11: RNA chain | Mass: 4437.700 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() Human adenovirus 2 |
| #15: RNA chain | Mass: 27772.039 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() Human adenovirus 2 |
-Protein , 18 types, 19 molecules 789ACDFGJKLOPSUVbki
| #4: Protein | Mass: 44691.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P38919 | ||
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| #5: Protein | Mass: 10370.526 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y5S9 | ||
| #6: Protein | Mass: 16929.314 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96A72 | ||
| #7: Protein | Mass: 273974.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q6P2Q9 | ||
| #9: Protein | Mass: 101231.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q15029 | ||
| #10: Protein | Mass: 14476.882 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9H875 | ||
| #12: Protein | Mass: 15210.249 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q8WUQ7 | ||
| #13: Protein | Mass: 7269.374 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y421 | ||
| #16: Protein | Mass: 35782.395 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O43660 | ||
| #17: Protein | Mass: 33819.922 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q13573 | ||
| #18: Protein | Mass: 17032.850 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P41223 | ||
| #21: Protein | Mass: 92406.883 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q99459 | ||
| #22: Protein | Mass: 26674.447 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9P013 | ||
| #24: Protein | Mass: 100610.008 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BZJ0 | ||
| #26: Protein | Mass: 171502.453 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O60306, RNA helicase | ||
| #27: Protein | Mass: 139522.312 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DHX8, DDX8 / Production host: ![]() | ||
| #31: Protein | Mass: 9551.284 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P14678#38: Protein | | Mass: 18055.529 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y3C6, peptidylprolyl isomerase |
-U5 small nuclear ribonucleoprotein ... , 2 types, 2 molecules BN
| #8: Protein | Mass: 197053.984 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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| #20: Protein | Mass: 34092.410 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96DI7 |
-Pre-mRNA-splicing factor ... , 6 types, 6 molecules HMTcsy
| #14: Protein | Mass: 105646.578 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9HCG8 |
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| #19: Protein | Mass: 33156.129 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9NW64 |
| #25: Protein | Mass: 100148.711 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9HCS7 |
| #32: Protein | Mass: 68510.844 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95391 |
| #41: Protein | Mass: 26163.420 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O75934 |
| #43: Protein | Mass: 17302.371 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95926 |
-Protein/peptide , 3 types, 3 molecules RZz
| #23: Protein/peptide | Mass: 2767.128 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9UQ35 |
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| #30: Protein/peptide | Mass: 3321.766 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q8N5F7 |
| #44: Protein/peptide | Mass: 4036.538 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q6IQ49 |
-U2 small nuclear ribonucleoprotein ... , 2 types, 2 molecules WY
| #28: Protein | Mass: 18697.730 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P09661 |
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| #29: Protein | Mass: 10688.563 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 dnepfqgrhljm
| #33: Protein | Mass: 9460.979 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62318#34: Protein | Mass: 9582.185 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62304#35: Protein | Mass: 8038.415 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62306#36: Protein | Mass: 8160.629 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62308#37: Protein | Mass: 9086.731 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62314#39: Protein | Mass: 13551.928 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62316 |
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-Pre-mRNA-processing factor ... , 2 types, 5 molecules otuvw
| #40: Protein | Mass: 59116.055 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O60508 |
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| #42: 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 |
-Non-polymers , 6 types, 18 molecules 










| #45: Chemical | ChemComp-MG / #46: Chemical | ChemComp-K / | #47: Chemical | ChemComp-ATP / | #48: Chemical | ChemComp-GTP / | #49: Chemical | ChemComp-ZN / #50: Chemical | ChemComp-IHP / | |
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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
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| Molecular weight | Value: 3.0 MDa / Experimental value: NO | ||||||||||||||||||||||||||||||
| Source (natural) |
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| Source (recombinant) |
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| Buffer solution | pH: 7.9 | ||||||||||||||||||||||||||||||
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| Specimen | Conc.: 0.3 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
| Specimen support | Grid type: Quantifoil R2/2 | ||||||||||||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK III / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K Details: 3 uL sample was applied to the grid, left for 25s, then blotted for 2.5-3.5s and immediately plunged into liquid 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 magnification: 135000 X / Nominal defocus max: 3500 nm / Nominal defocus min: 1500 nm / Cs: 2.7 mm |
| Image recording | Average exposure time: 10 sec. / Electron dose: 53 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 2 / Num. of real images: 6200 |
| Image scans | Movie frames/image: 40 / Used frames/image: 1-40 |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 103860 / Symmetry type: POINT |
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About Yorodumi




Homo sapiens (human)
Human adenovirus 2
United Kingdom, 2items
Citation
UCSF Chimera
















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