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Open data
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Basic information
| Entry | Database: PDB / ID: 7abg | ||||||
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| Title | Human pre-Bact-1 spliceosome | ||||||
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Keywords | SPLICING / Complex / spliceosome / catalytic activation | ||||||
| Function / homology | Function and homology informationprotein localization to P-body / positive regulation of RNA binding / snRNA export from nucleus / DNA topoisomerase binding / RS domain binding / nuclear cap binding complex / histone mRNA metabolic process / RNA cap binding complex / microfibril / mRNA metabolic process ...protein localization to P-body / positive regulation of RNA binding / snRNA export from nucleus / DNA topoisomerase binding / RS domain binding / nuclear cap binding complex / histone mRNA metabolic process / RNA cap binding complex / microfibril / mRNA metabolic process / Lsm2-8 complex / U6 snRNA 3'-end binding / positive regulation of RNA export from nucleus / mRNA decay by 5' to 3' exoribonuclease / Lsm1-7-Pat1 complex / protein kinase B binding / positive regulation of mRNA 3'-end processing / cap-dependent translational initiation / U6 snRNP / Processing of Intronless Pre-mRNAs / U11/U12 snRNP / PH domain binding / regulation of retinoic acid receptor signaling pathway / U2 snRNP binding / interleukin-17-mediated signaling pathway / U7 snRNA binding / histone pre-mRNA DCP binding / RNA cap binding / U7 snRNP / snRNA binding / histone pre-mRNA 3'end processing complex / cis assembly of pre-catalytic spliceosome / regulation of mRNA processing / primary miRNA processing / miRNA-mediated post-transcriptional gene silencing / regulation of vitamin D receptor signaling pathway / mRNA splice site recognition / SLBP independent Processing of Histone Pre-mRNAs / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs / spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) / regulatory ncRNA-mediated post-transcriptional gene silencing / B-WICH complex / miRNA processing / nuclear retinoic acid receptor binding / protein methylation / RNA 7-methylguanosine cap binding / Transport of the SLBP independent Mature mRNA / U12-type spliceosomal complex / Transport of the SLBP Dependant Mature mRNA / alternative mRNA splicing, via spliceosome / 7-methylguanosine cap hypermethylation / U1 snRNP binding / methylosome / mRNA 3'-end processing / pICln-Sm protein complex / U2-type catalytic step 1 spliceosome / RNA splicing, via transesterification reactions / snRNP binding / Transport of Mature mRNA Derived from an Intronless Transcript / pre-mRNA binding / regulation of mRNA splicing, via spliceosome / positive regulation of mRNA splicing, via spliceosome / transcription elongation factor activity / blastocyst formation / small nuclear ribonucleoprotein complex / sno(s)RNA-containing ribonucleoprotein complex / SMN-Sm protein complex / splicing factor binding / spliceosomal tri-snRNP complex / Notch binding / host-mediated activation of viral transcription / mRNA 3'-end processing / P granule / mRNA stabilization / telomerase holoenzyme complex / U2-type precatalytic spliceosome / commitment complex / mRNA cis splicing, via spliceosome / positive regulation of vitamin D receptor signaling pathway / telomerase RNA binding / U2-type prespliceosome assembly / U2-type spliceosomal complex / nuclear vitamin D receptor binding / RNA polymerase binding / U2-type catalytic step 2 spliceosome / Transport of Mature mRNA derived from an Intron-Containing Transcript / Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells / RUNX3 regulates NOTCH signaling / NOTCH4 Intracellular Domain Regulates Transcription / RNA catabolic process / U2 snRNP / P-body assembly / signal transduction involved in regulation of gene expression / RNA Polymerase II Transcription Termination / SAGA complex / U1 snRNP / RHOBTB1 GTPase cycle / Abortive elongation of HIV-1 transcript in the absence of Tat / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / U4 snRNP Similarity search - Function | ||||||
| Biological species | Homo sapiens (human)synthetic construct (others) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 7.8 Å | ||||||
Authors | Townsend, C. / Kastner, B. / Leelaram, M.N. / Bertram, K. / Stark, H. / Luehrmann, R. | ||||||
| Funding support | Germany, 1items
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Citation | Journal: Science / Year: 2020Title: Mechanism of protein-guided folding of the active site U2/U6 RNA during spliceosome activation. Authors: Cole Townsend / Majety N Leelaram / Dmitry E Agafonov / Olexandr Dybkov / Cindy L Will / Karl Bertram / Henning Urlaub / Berthold Kastner / Holger Stark / Reinhard Lührmann / ![]() Abstract: Spliceosome activation involves extensive protein and RNA rearrangements that lead to formation of a catalytically active U2/U6 RNA structure. At present, little is known about the assembly pathway ...Spliceosome activation involves extensive protein and RNA rearrangements that lead to formation of a catalytically active U2/U6 RNA structure. At present, little is known about the assembly pathway of the latter and the mechanism whereby proteins aid its proper folding. Here, we report the cryo-electron microscopy structures of two human, activated spliceosome precursors (that is, pre-B complexes) at core resolutions of 3.9 and 4.2 angstroms. These structures elucidate the order of the numerous protein exchanges that occur during activation, the mutually exclusive interactions that ensure the correct order of ribonucleoprotein rearrangements needed to form the U2/U6 catalytic RNA, and the stepwise folding pathway of the latter. Structural comparisons with mature B complexes reveal the molecular mechanism whereby a conformational change in the scaffold protein PRP8 facilitates final three-dimensional folding of the U2/U6 catalytic RNA. | ||||||
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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 | 7abg.cif.gz | 2.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7abg.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 7abg.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7abg_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
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| Full document | 7abg_full_validation.pdf.gz | 1.6 MB | Display | |
| Data in XML | 7abg_validation.xml.gz | 251.1 KB | Display | |
| Data in CIF | 7abg_validation.cif.gz | 447.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ab/7abg ftp://data.pdbj.org/pub/pdb/validation_reports/ab/7abg | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 11695MC ![]() 7aavC ![]() 7abfC ![]() 7abhC ![]() 7abiC M: map data used to model this data C: citing same article ( |
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| Similar structure data | |
| EM raw data | EMPIAR-10616 (Title: Cryo-EM dataset of human pre-Bact spliceosome / Data size: 584.5 Data #1: Motion-corrected micrographs (without dose-weighting) of human pre-Bact spliceosome [micrographs - single frame] Data #2: Motion-corrected micrographs (with dose-weighting) of human pre-Bact spliceosome [micrographs - single frame]) |
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Links
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Assembly
| Deposited unit | ![]()
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Components
+Nuclear cap-binding protein subunit ... , 2 types, 2 molecules A5A1
+U6 snRNA-associated Sm-like protein ... , 7 types, 7 molecules A2V9CHJA3
+Splicing factor 3B subunit ... , 6 types, 6 molecules zuTEwx
+Splicing factor 3A subunit ... , 3 types, 3 molecules Fp4
+U5 small nuclear ribonucleoprotein ... , 2 types, 2 molecules Ds
+U2 small nuclear ribonucleoprotein ... , 2 types, 2 molecules WB
+Protein , 17 types, 18 molecules QLRKyGAA4v0NrYA6mfqX
+RNA chain , 4 types, 4 molecules 52Z6
+Pre-mRNA-splicing factor ... , 2 types, 2 molecules IP
+Small nuclear ribonucleoprotein ... , 6 types, 12 molecules haiblekdjcng
+Non-polymers , 4 types, 4 molecules 






+Details
-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 | Units: MEGADALTONS / Experimental value: NO | ||||||||||||||||||
| Source (natural) | Organism: Homo sapiens (human) | ||||||||||||||||||
| Source (recombinant) | Organism: synthetic construct (others) | ||||||||||||||||||
| Buffer solution | pH: 7.9 | ||||||||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||
| Specimen support | Grid material: COPPER / Grid type: Quantifoil R3.5/1 | ||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / 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: SPOT SCAN |
| Electron lens | Mode: BRIGHT FIELD |
| Image recording | Average exposure time: 1 sec. / Electron dose: 2.25 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON III (4k x 4k) |
| Image scans | Width: 4096 / Height: 4096 |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||
| 3D reconstruction | Resolution: 7.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 84539 / Symmetry type: POINT | ||||||||||||||||||||
| Atomic model building | Protocol: RIGID BODY FIT / Space: REAL |
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About Yorodumi




Homo sapiens (human)
Germany, 1items
Citation
UCSF Chimera














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