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Yorodumi- EMDB-6891: Cryo-EM structure of a human activated spliceosome (early Bact) a... -
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Basic information
| Entry | Database: EMDB / ID: EMD-6891 | ||||||||||||
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| Title | Cryo-EM structure of a human activated spliceosome (early Bact) at 4.9 angstrom. | ||||||||||||
Map data | Cryo-EM structure of the human activated spliceosome (early Bact) at 4.8 angstrom | ||||||||||||
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Keywords | spliceosome / cryo-EM structure / activated spliceosome / early Bact complex / pre-mRNA splicing / SPLICING | ||||||||||||
| Function / homology | Function and homology informationRES complex / negative regulation of chemokine-mediated signaling pathway / regulation of vitamin D receptor signaling pathway / 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 / U7 snRNP ...RES complex / negative regulation of chemokine-mediated signaling pathway / regulation of vitamin D receptor signaling pathway / 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 / U7 snRNP / cis assembly of pre-catalytic spliceosome / histone pre-mRNA 3'end processing complex / nuclear histone mRNA catabolic process / SLBP independent Processing of Histone Pre-mRNAs / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs / miRNA processing / 7-methylguanosine cap hypermethylation / U12-type spliceosomal complex / positive regulation of mRNA splicing, via spliceosome / nuclear retinoic acid receptor binding / U1 snRNP binding / pICln-Sm protein complex / U2-type catalytic step 1 spliceosome / methylosome / regulation of mRNA splicing, via spliceosome / RNA splicing, via transesterification reactions / sno(s)RNA-containing ribonucleoprotein complex / small nuclear ribonucleoprotein complex / splicing factor binding / SMN-Sm protein complex / spliceosomal tri-snRNP complex / positive regulation of vitamin D receptor signaling pathway / commitment complex / P granule / U4 snRNP / snRNP binding / host-mediated activation of viral transcription / U2-type precatalytic spliceosome / mRNA cis splicing, via spliceosome / Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells / U2-type prespliceosome assembly / RUNX3 regulates NOTCH signaling / U2-type catalytic step 2 spliceosome / Notch binding / U2-type spliceosomal complex / nuclear vitamin D receptor binding / telomerase holoenzyme complex / NOTCH4 Intracellular Domain Regulates Transcription / telomerase RNA binding / pre-mRNA binding / positive regulation of neurogenesis / U1 snRNP / U2 snRNP / spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) / RNA Polymerase II Transcription Termination / NOTCH3 Intracellular Domain Regulates Transcription / protein methylation / mRNA stabilization / U2-type prespliceosome / K63-linked polyubiquitin modification-dependent protein binding / nuclear androgen receptor binding / precatalytic spliceosome / Notch-HLH transcription pathway / Formation of paraxial mesoderm / pattern recognition receptor activity / positive regulation of transforming growth factor beta receptor signaling pathway / WD40-repeat domain binding / mRNA 3'-splice site recognition / regulation of RNA splicing / SMAD binding / positive regulation of transcription by RNA polymerase III / mRNA Splicing - Minor Pathway / positive regulation of transcription by RNA polymerase I / spliceosomal complex assembly / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / Prp19 complex / negative regulation of mRNA splicing, via spliceosome / spliceosomal tri-snRNP complex assembly / U5 snRNP / U5 snRNA binding / pre-mRNA intronic binding / U2 snRNA binding / U6 snRNA binding / U4/U6 x U5 tri-snRNP complex / Cajal body / U1 snRNA binding / retinoic acid receptor signaling pathway / transcription regulator inhibitor activity / RNA processing / cellular response to retinoic acid / DNA damage checkpoint signaling / spliceosomal snRNP assembly / stem cell differentiation / catalytic step 2 spliceosome / spliceosomal complex / mRNA Splicing - Major Pathway / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / RNA splicing / regulation of DNA repair / nuclear receptor binding Similarity search - Function | ||||||||||||
| Biological species | Homo sapiens (human) / unidentified adenovirus | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 4.9 Å | ||||||||||||
Authors | Zhang X / Yan C | ||||||||||||
| Funding support | China, 3 items
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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
| Movie |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_6891.map.gz | 226.9 MB | EMDB map data format | |
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| Header (meta data) | emd-6891-v30.xml emd-6891.xml | 64.9 KB 64.9 KB | Display Display | EMDB header |
| Images | emd_6891.png | 163.3 KB | ||
| Filedesc metadata | emd-6891.cif.gz | 20.5 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-6891 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-6891 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 5z58MC ![]() 6889C ![]() 6890C ![]() 5z56C ![]() 5z57C C: citing same article ( M: atomic model generated by this map |
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| Similar structure data |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_6891.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Annotation | Cryo-EM structure of the human activated spliceosome (early Bact) at 4.8 angstrom | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.338 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
+Entire : early Bact spliceosome
+Supramolecule #1: early Bact spliceosome
+Macromolecule #1: Pre-mRNA-processing-splicing factor 8
+Macromolecule #3: 116 kDa U5 small nuclear ribonucleoprotein component
+Macromolecule #4: U5 small nuclear ribonucleoprotein 200 kDa helicase
+Macromolecule #5: U5 small nuclear ribonucleoprotein 40 kDa protein
+Macromolecule #6: Small nuclear ribonucleoprotein Sm D3
+Macromolecule #7: Small nuclear ribonucleoprotein-associated proteins B and B'
+Macromolecule #8: Small nuclear ribonucleoprotein Sm D1
+Macromolecule #9: Small nuclear ribonucleoprotein Sm D2
+Macromolecule #10: Small nuclear ribonucleoprotein F
+Macromolecule #11: Small nuclear ribonucleoprotein E
+Macromolecule #12: Small nuclear ribonucleoprotein G
+Macromolecule #16: U2 small nuclear ribonucleoprotein A'
+Macromolecule #17: U2 small nuclear ribonucleoprotein B''
+Macromolecule #18: Splicing factor 3A subunit 3
+Macromolecule #19: Splicing factor 3A subunit 1
+Macromolecule #20: Splicing factor 3A subunit 2
+Macromolecule #21: Splicing factor 3B subunit 1
+Macromolecule #22: Splicing factor 3B subunit 2
+Macromolecule #23: Splicing factor 3B subunit 3
+Macromolecule #24: Splicing factor 3B subunit 4
+Macromolecule #25: Splicing factor 3B subunit 6
+Macromolecule #26: PHD finger-like domain-containing protein 5A
+Macromolecule #27: Splicing factor 3B subunit 5
+Macromolecule #28: Crooked neck-like protein 1
+Macromolecule #29: Cell division cycle 5-like protein
+Macromolecule #30: RING finger protein 113A
+Macromolecule #31: Spliceosome-associated protein CWC15 homolog
+Macromolecule #32: Skip
+Macromolecule #33: Pleiotropic regulator 1
+Macromolecule #34: Pre-mRNA-splicing factor CWC22 homolog
+Macromolecule #35: Smad nuclear-interacting protein 1
+Macromolecule #36: RNA-binding motif protein, X-linked 2
+Macromolecule #37: BUD13 homolog
+Macromolecule #38: Peptidyl-prolyl cis-trans isomerase CWC27 homolog
+Macromolecule #39: Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16
+Macromolecule #2: U5 snRNA
+Macromolecule #13: U6 snRNA
+Macromolecule #14: pre-mRNA
+Macromolecule #15: U2 snRNA
+Macromolecule #40: INOSITOL HEXAKISPHOSPHATE
+Macromolecule #41: GUANOSINE-5'-TRIPHOSPHATE
+Macromolecule #42: MAGNESIUM ION
+Macromolecule #43: ZINC ION
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.9 / Details: 20 mM HEPES-KOH, pH 7.9, 150 mM NaCl, 1.5 mM MgCl2 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 48.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi


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










































Z (Sec.)
Y (Row.)
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Processing
