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Yorodumi- PDB-5z57: Cryo-EM structure of the human activated spliceosome (late Bact) ... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 5z57 | ||||||||||||
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| Title | Cryo-EM structure of the human activated spliceosome (late Bact) at 6.5 angstrom | ||||||||||||
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Keywords | SPLICING / spliceosome / cryo-EM structure / activated spliceosome / late Bact complex / pre-mRNA splicing | ||||||||||||
| Function / homology | Function and homology informationRES complex / U11/U12 snRNP / post-mRNA release spliceosomal complex / U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / generation of catalytic spliceosome for first transesterification step / U7 snRNP / 3'-5' RNA helicase activity / cis assembly of pre-catalytic spliceosome ...RES complex / U11/U12 snRNP / post-mRNA release spliceosomal complex / U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / generation of catalytic spliceosome for first transesterification step / U7 snRNP / 3'-5' RNA helicase activity / cis assembly of pre-catalytic spliceosome / histone pre-mRNA 3'end processing complex / SLBP independent Processing of Histone Pre-mRNAs / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs / B-WICH complex / miRNA processing / oocyte development / alternative mRNA splicing, via spliceosome / poly(A) binding / 7-methylguanosine cap hypermethylation / U12-type spliceosomal complex / protein methylation / spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) / U1 snRNP binding / pre-mRNA binding / U2-type catalytic step 1 spliceosome / pICln-Sm protein complex / C2H2 zinc finger domain binding / methylosome / regulation of mRNA splicing, via spliceosome / embryonic brain development / positive regulation of mRNA splicing, via spliceosome / RNA splicing, via transesterification reactions / mRNA 3'-end processing / sno(s)RNA-containing ribonucleoprotein complex / small nuclear ribonucleoprotein complex / SMN-Sm protein complex / spliceosomal tri-snRNP complex / splicing factor binding / blastocyst formation / P granule / snRNP binding / commitment complex / U2-type precatalytic spliceosome / mRNA cis splicing, via spliceosome / U2-type prespliceosome assembly / U2-type catalytic step 2 spliceosome / U2-type spliceosomal complex / Transport of Mature mRNA derived from an Intron-Containing Transcript / telomerase holoenzyme complex / inner cell mass cell proliferation / telomerase RNA binding / U1 snRNP / SAGA complex / U2 snRNP / RNA Polymerase II Transcription Termination / U4 snRNP / U2-type prespliceosome / positive regulation of transcription by RNA polymerase III / protein peptidyl-prolyl isomerization / K63-linked polyubiquitin modification-dependent protein binding / mRNA stabilization / cyclosporin A binding / ubiquitin-ubiquitin ligase activity / precatalytic spliceosome / lipid biosynthetic process / pattern recognition receptor activity / WD40-repeat domain binding / mRNA 3'-splice site recognition / blastocyst development / regulation of RNA splicing / mRNA Splicing - Minor Pathway / positive regulation of transcription by RNA polymerase I / Dengue Virus-Host Interactions / spliceosomal complex assembly / negative regulation of mRNA splicing, via spliceosome / spliceosomal tri-snRNP complex assembly / Prp19 complex / U5 snRNP / U5 snRNA binding / pre-mRNA intronic binding / U2 snRNA binding / U6 snRNA binding / protein K63-linked ubiquitination / spliceosomal snRNP assembly / protein localization to nucleus / Cajal body / U1 snRNA binding / regulation of DNA repair / RNA processing / positive regulation of G1/S transition of mitotic cell cycle / U4/U6 x U5 tri-snRNP complex / transcription regulator inhibitor activity / positive regulation of viral genome replication / ovarian follicle development / spindle assembly / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / DNA damage checkpoint signaling / lipid droplet / transcription-coupled nucleotide-excision repair Similarity search - Function | ||||||||||||
| Biological species | Homo sapiens (human) unidentified adenovirus | ||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 6.5 Å | ||||||||||||
Authors | Zhang, X. / Yan, C. / Zhan, X. / Li, L. / Lei, J. / Shi, Y. | ||||||||||||
| Funding support | China, 3items
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Citation | Journal: Cell Res / Year: 2018Title: Structure of the human activated spliceosome in three conformational states. Authors: Xiaofeng Zhang / Chuangye Yan / Xiechao Zhan / Lijia Li / Jianlin Lei / Yigong Shi / ![]() Abstract: During each cycle of pre-mRNA splicing, the pre-catalytic spliceosome (B complex) is converted into the activated spliceosome (B complex), which has a well-formed active site but cannot proceed to ...During each cycle of pre-mRNA splicing, the pre-catalytic spliceosome (B complex) is converted into the activated spliceosome (B complex), which has a well-formed active site but cannot proceed to the branching reaction. Here, we present the cryo-EM structure of the human B complex in three distinct conformational states. The EM map allows atomic modeling of nearly all protein components of the U2 small nuclear ribonucleoprotein (snRNP), including three of the SF3a complex and seven of the SF3b complex. The structure of the human B complex contains 52 proteins, U2, U5, and U6 small nuclear RNA (snRNA), and a pre-mRNA. Three distinct conformations have been captured, representing the early, mature, and late states of the human B complex. These complexes differ in the orientation of the Switch loop of Prp8, the splicing factors RNF113A and NY-CO-10, and most components of the NineTeen complex (NTC) and the NTC-related complex. Analysis of these three complexes and comparison with the B and C complexes reveal an ordered flux of components in the B-to-B and the B-to-B transitions, which ultimately prime the active site for the branching reaction. | ||||||||||||
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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 | 5z57.cif.gz | 3.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb5z57.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 5z57.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z5/5z57 ftp://data.pdbj.org/pub/pdb/validation_reports/z5/5z57 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 6890MC ![]() 6889C ![]() 6891C ![]() 5z56C ![]() 5z58C 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
+Protein , 15 types, 16 molecules ACbi6JLQNPRTUXYZ
+RNA chain , 4 types, 4 molecules BFGH
+U5 small nuclear ribonucleoprotein ... , 2 types, 2 molecules DE
+Small nuclear ribonucleoprotein ... , 6 types, 12 molecules ahcjdkfmelgn
+U2 small nuclear ribonucleoprotein ... , 2 types, 2 molecules op
+Splicing factor 3A subunit ... , 3 types, 3 molecules wuv
+Splicing factor 3B subunit ... , 6 types, 6 molecules 123457
+Pre-mRNA-processing factor ... , 2 types, 5 molecules qrstW
+Pre-mRNA-splicing factor ... , 5 types, 5 molecules KIOVx
+Peptidyl-prolyl cis-trans ... , 2 types, 2 molecules Sy
+Non-polymers , 5 types, 19 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: late Bact splieosome / Type: COMPLEX / Entity ID: #1-#47 / Source: NATURAL |
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| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.9 / Details: 20 mM HEPES-KOH, pH 7.9, 150 mM NaCl, 1.5 mM MgCl2 |
| 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 / Cs: 2.7 mm / Alignment procedure: BASIC |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 48 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
| EM imaging optics | Energyfilter name: GIF Quantum LS |
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Processing
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| CTF correction | Type: NONE | ||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 6.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 14316 / Algorithm: FOURIER SPACE / Symmetry type: POINT | ||||||||||||||||||||||||||||
| Refinement | Highest resolution: 6.5 Å |
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About Yorodumi



Homo sapiens (human)
unidentified adenovirus
China, 3items
Citation
UCSF Chimera













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