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Open data
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Basic information
Entry | Database: PDB / ID: 8i0r | ||||||
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Title | The cryo-EM structure of human Bact-I complex | ||||||
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![]() | SPLICING / spliceosome / Bact-I complex / RNA splicing / PRP2 / activation | ||||||
Function / homology | ![]() RES complex / negative regulation of chemokine-mediated signaling pathway / snoRNA splicing / U11/U12 snRNP / regulation of retinoic acid receptor signaling pathway / post-mRNA release spliceosomal complex / U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / 3'-5' RNA helicase activity ...RES complex / negative regulation of chemokine-mediated signaling pathway / snoRNA splicing / U11/U12 snRNP / regulation of retinoic acid receptor signaling pathway / post-mRNA release spliceosomal complex / U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / 3'-5' RNA helicase activity / U7 snRNP / regulation of vitamin D receptor signaling pathway / generation of catalytic spliceosome for first transesterification step / histone pre-mRNA 3'end processing complex / cis assembly of pre-catalytic spliceosome / positive regulation of androgen receptor activity / SLBP independent Processing of Histone Pre-mRNAs / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs / B-WICH complex / miRNA processing / nuclear retinoic acid receptor binding / splicing factor binding / spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) / protein methylation / U12-type spliceosomal complex / poly(A) binding / 7-methylguanosine cap hypermethylation / mRNA 3'-end processing / sno(s)RNA-containing ribonucleoprotein complex / U1 snRNP binding / RNA splicing, via transesterification reactions / methylosome / blastocyst formation / pICln-Sm protein complex / C2H2 zinc finger domain binding / regulation of mRNA splicing, via spliceosome / positive regulation of mRNA splicing, via spliceosome / U2-type catalytic step 1 spliceosome / pre-mRNA binding / snRNP binding / small nuclear ribonucleoprotein complex / telomerase RNA binding / telomerase holoenzyme complex / SMN-Sm protein complex / P granule / positive regulation by host of viral transcription / spliceosomal tri-snRNP complex / positive regulation of vitamin D receptor signaling pathway / U2-type precatalytic spliceosome / nuclear vitamin D receptor binding / U2-type spliceosomal complex / mRNA cis splicing, via spliceosome / commitment complex / U2-type prespliceosome assembly / Transport of Mature mRNA derived from an Intron-Containing Transcript / Notch binding / Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells / RUNX3 regulates NOTCH signaling / U2-type catalytic step 2 spliceosome / NOTCH4 Intracellular Domain Regulates Transcription / SAGA complex / U4 snRNP / RHOBTB1 GTPase cycle / RNA Polymerase II Transcription Termination / U2 snRNP / U1 snRNP / NOTCH3 Intracellular Domain Regulates Transcription / positive regulation of transcription by RNA polymerase III / WD40-repeat domain binding / Basigin interactions / U2-type prespliceosome / positive regulation of neurogenesis / ubiquitin-ubiquitin ligase activity / K63-linked polyubiquitin modification-dependent protein binding / nuclear androgen receptor binding / precatalytic spliceosome / cyclosporin A binding / Notch-HLH transcription pathway / pattern recognition receptor activity / transcription regulator inhibitor activity / positive regulation of transforming growth factor beta receptor signaling pathway / Formation of paraxial mesoderm / positive regulation of transcription by RNA polymerase I / SMAD binding / spliceosomal complex assembly / regulation of RNA splicing / mRNA Splicing - Minor Pathway / mRNA 3'-splice site recognition / spliceosomal tri-snRNP complex assembly / blastocyst development / Prp19 complex / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / U5 snRNA binding / positive regulation of G1/S transition of mitotic cell cycle / protein localization to nucleus / U5 snRNP / U2 snRNA binding / U6 snRNA binding / RNA processing / pre-mRNA intronic binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å | ||||||
![]() | Zhan, X. / Lu, Y. / Shi, Y. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Molecular basis for the activation of human spliceosome. Authors: Xiechao Zhan / Yichen Lu / Yigong Shi / ![]() Abstract: The spliceosome executes pre-mRNA splicing through four sequential stages: assembly, activation, catalysis, and disassembly. Activation of the spliceosome, namely remodeling of the pre-catalytic ...The spliceosome executes pre-mRNA splicing through four sequential stages: assembly, activation, catalysis, and disassembly. Activation of the spliceosome, namely remodeling of the pre-catalytic spliceosome (B complex) into the activated spliceosome (B complex) and the catalytically activated spliceosome (B complex), involves major flux of protein components and structural rearrangements. Relying on a splicing inhibitor, we have captured six intermediate states between the B and B complexes: pre-B, B-I, B-II, B-III, B-IV, and post-B. Their cryo-EM structures, together with an improved structure of the catalytic step I spliceosome (C complex), reveal how the catalytic center matures around the internal stem loop of U6 snRNA, how the branch site approaches 5'-splice site, how the RNA helicase PRP2 rearranges to bind pre-mRNA, and how U2 snRNP undergoes remarkable movement to facilitate activation. We identify a previously unrecognized key role of PRP2 in spliceosome activation. Our study recapitulates a molecular choreography of the human spliceosome during its catalytic activation. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 3 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 2.1 MB | Display | ![]() |
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Full document | ![]() | 2.5 MB | Display | |
Data in XML | ![]() | 388.7 KB | Display | |
Data in CIF | ![]() | 643.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 35107MC ![]() 8i0pC ![]() 8i0sC ![]() 8i0tC ![]() 8i0uC ![]() 8i0vC ![]() 8i0wC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
+Protein , 17 types, 18 molecules ACJKLNPQRTWXYZ79ma
+RNA chain , 4 types, 4 molecules BFGH
+U5 small nuclear ribonucleoprotein ... , 2 types, 2 molecules DE
+Pre-mRNA-splicing factor ... , 4 types, 4 molecules IOSV
+Serine/arginine repetitive matrix protein ... , 2 types, 2 molecules U8
+Splicing factor 3B subunit ... , 6 types, 6 molecules 132465
+U2 small nuclear ribonucleoprotein ... , 2 types, 2 molecules po
+Splicing factor 3A subunit ... , 3 types, 3 molecules wuv
+Peptidyl-prolyl cis-trans isomerase ... , 2 types, 2 molecules yz
+Small nuclear ribonucleoprotein ... , 6 types, 12 molecules hcidlgkfjenb
+Non-polymers , 4 types, 15 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
Component | Name: The human Bact-I complex / Type: COMPLEX Entity ID: #1-#5, #21, #11, #25, #6, #8, #26-#27, #10, #12, #15, #28-#29, #16, #9, #30-#32, #24, #23, #33-#35, #17, #19, #36-#47, #7, #48, #14, #13, #20, #18, #22 Source: NATURAL |
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Source (natural) | Organism: ![]() |
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: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1400 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
Software | Name: PHENIX / Version: 1.17.1_3660: / Classification: refinement | ||||||||||||||||||||||||
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CTF correction | Type: NONE | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 136665 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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