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Open data
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Basic information
| Entry | ![]() | ||||||||||||||||||
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| Title | Human debranched intron spliceosome (DIS) | ||||||||||||||||||
Map data | Composite map | ||||||||||||||||||
Sample |
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Keywords | Spliceosome / complex / SPLICING | ||||||||||||||||||
| Function / homology | Function and homology informationregulation of vitamin D receptor signaling pathway / regulation of retinoic acid receptor signaling pathway / U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / U7 snRNP / generation of catalytic spliceosome for first transesterification step / 3'-5' RNA helicase activity / cis assembly of pre-catalytic spliceosome / histone pre-mRNA 3'end processing complex ...regulation of vitamin D receptor signaling pathway / regulation of retinoic acid receptor signaling pathway / U2 snRNP binding / U7 snRNA binding / histone pre-mRNA DCP binding / U7 snRNP / generation of catalytic spliceosome for first transesterification step / 3'-5' RNA helicase activity / cis assembly of pre-catalytic spliceosome / histone pre-mRNA 3'end processing complex / U4atac snRNP / SLBP independent Processing of Histone Pre-mRNAs / nuclear histone mRNA catabolic process / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs / U4atac/U6atac snRNP / U11/U12 snRNP / poly(A) binding / U4atac/U6atac x U5 tri-snRNP complex / 7-methylguanosine cap hypermethylation / U12-type spliceosomal complex / embryonic brain development / U1 snRNP binding / nuclear retinoic acid receptor binding / positive regulation of mRNA splicing, via spliceosome / RNA splicing, via transesterification reactions / pICln-Sm protein complex / snRNP binding / RNA Polymerase II Transcription Termination / mRNA 3'-end processing / sno(s)RNA-containing ribonucleoprotein complex / methylosome / small nuclear ribonucleoprotein complex / U12-type catalytic step 2 spliceosome / post-spliceosomal complex / SMN-Sm protein complex / spliceosomal tri-snRNP complex / positive regulation of vitamin D receptor signaling pathway / U12-type precatalytic spliceosome / P granule / commitment complex / host-mediated activation of viral transcription / U2-type precatalytic spliceosome / post-mRNA release spliceosomal complex / Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells / RUNX3 regulates NOTCH signaling / Notch binding / U2-type spliceosomal complex / telomerase holoenzyme complex / nuclear vitamin D receptor binding / Transport of Mature mRNA derived from an Intron-Containing Transcript / U2-type prespliceosome assembly / NOTCH4 Intracellular Domain Regulates Transcription / telomerase RNA binding / pre-mRNA binding / U4/U6 snRNP / U2-type catalytic step 2 spliceosome / positive regulation of neurogenesis / U1 snRNP / protein methylation / spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) / U2 snRNP / NOTCH3 Intracellular Domain Regulates Transcription / U4 snRNP / mRNA stabilization / U2-type prespliceosome / U2-type catalytic step 1 spliceosome / protein peptidyl-prolyl isomerization / cyclosporin A binding / nuclear androgen receptor binding / K63-linked polyubiquitin modification-dependent protein binding / generation of catalytic spliceosome for second transesterification step / ubiquitin-ubiquitin ligase activity / Notch-HLH transcription pathway / Formation of paraxial mesoderm / positive regulation of transforming growth factor beta receptor signaling pathway / mRNA 3'-splice site recognition / WD40-repeat domain binding / SMAD binding / mRNA Splicing - Minor Pathway / spliceosomal complex assembly / precatalytic spliceosome / intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / Prp19 complex / negative regulation of mRNA splicing, via spliceosome / U5 snRNA binding / spliceosomal tri-snRNP complex assembly / U5 snRNP / U6 snRNA binding / RNA splicing / mRNA cis splicing, via spliceosome / U4/U6 x U5 tri-snRNP complex / cellular response to retinoic acid / Cajal body / retinoic acid receptor signaling pathway / RNA processing / positive regulation of viral genome replication / DNA damage checkpoint signaling / spliceosomal snRNP assembly / positive regulation of protein export from nucleus / catalytic step 2 spliceosome Similarity search - Function | ||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.14 Å | ||||||||||||||||||
Authors | Boreikaite V / Vorlaender MK / Plaschka C | ||||||||||||||||||
| Funding support | European Union, France, Austria, 5 items
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Citation | Journal: Acta Crystallogr D Struct Biol / Year: 2019 Title: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty ...Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty / Robert D Oeffner / Billy K Poon / Michael G Prisant / Randy J Read / Jane S Richardson / David C Richardson / Massimo D Sammito / Oleg V Sobolev / Duncan H Stockwell / Thomas C Terwilliger / Alexandre G Urzhumtsev / Lizbeth L Videau / Christopher J Williams / Paul D Adams / ![]() Abstract: Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological ...Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological processes and to develop new therapeutics against diseases. The overall structure-solution workflow is similar for these techniques, but nuances exist because the properties of the reduced experimental data are different. Software tools for structure determination should therefore be tailored for each method. Phenix is a comprehensive software package for macromolecular structure determination that handles data from any of these techniques. Tasks performed with Phenix include data-quality assessment, map improvement, model building, the validation/rebuilding/refinement cycle and deposition. Each tool caters to the type of experimental data. The design of Phenix emphasizes the automation of procedures, where possible, to minimize repetitive and time-consuming manual tasks, while default parameters are chosen to encourage best practice. A graphical user interface provides access to many command-line features of Phenix and streamlines the transition between programs, project tracking and re-running of previous tasks. | ||||||||||||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_54494.map.gz | 10.9 MB | EMDB map data format | |
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| Header (meta data) | emd-54494-v30.xml emd-54494.xml | 67.5 KB 67.5 KB | Display Display | EMDB header |
| Images | emd_54494.png | 151.8 KB | ||
| Filedesc metadata | emd-54494.cif.gz | 19.2 KB | ||
| Archive directory | https://data.pdbj.org/pub/emdb/structures/EMD-54494 ftp://data.pdbj.org/pub/emdb/structures/EMD-54494 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9s2fMC ![]() 9s2eC ![]() 9s2gC C: citing same article ( M: atomic model generated by this map |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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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_54494.map.gz / Format: CCP4 / Size: 343 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Composite map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.1887 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
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Sample components
+Entire : Debranched intron spliceosome complex
+Supramolecule #1: Debranched intron spliceosome complex
+Macromolecule #1: Probable ATP-dependent RNA helicase DHX35
+Macromolecule #3: Pre-mRNA-processing-splicing factor 8
+Macromolecule #4: U5 small nuclear ribonucleoprotein 200 kDa helicase
+Macromolecule #5: 116 kDa U5 small nuclear ribonucleoprotein component
+Macromolecule #6: U5 small nuclear ribonucleoprotein 40 kDa protein
+Macromolecule #7: G patch domain-containing protein 1
+Macromolecule #8: Pre-mRNA-splicing factor SYF1
+Macromolecule #9: Crooked neck-like protein 1
+Macromolecule #10: Pre-mRNA-splicing factor SPF27
+Macromolecule #11: Cell division cycle 5-like protein
+Macromolecule #12: Pre-mRNA-splicing factor SYF2
+Macromolecule #13: Protein BUD31 homolog
+Macromolecule #14: Pre-mRNA-splicing factor RBM22
+Macromolecule #15: Spliceosome-associated protein CWC15 homolog
+Macromolecule #16: Intron-binding protein aquarius
+Macromolecule #17: SNW domain-containing protein 1
+Macromolecule #18: Peptidyl-prolyl cis-trans isomerase-like 1
+Macromolecule #19: Pleiotropic regulator 1
+Macromolecule #20: Pre-mRNA-processing factor 17
+Macromolecule #21: WD repeat domain-containing protein 83
+Macromolecule #22: Coiled-coil domain-containing protein 12
+Macromolecule #23: Small nuclear ribonucleoprotein Sm D3
+Macromolecule #24: Small nuclear ribonucleoprotein-associated proteins B and B'
+Macromolecule #25: Small nuclear ribonucleoprotein Sm D1
+Macromolecule #26: Small nuclear ribonucleoprotein Sm D2
+Macromolecule #27: Small nuclear ribonucleoprotein E
+Macromolecule #28: Small nuclear ribonucleoprotein F
+Macromolecule #29: Small nuclear ribonucleoprotein G
+Macromolecule #30: Pre-mRNA-processing factor 19
+Macromolecule #31: Peptidyl-prolyl cis-trans isomerase E
+Macromolecule #32: Pre-mRNA-splicing factor ISY1 homolog
+Macromolecule #2: U5 snRNA
+Macromolecule #33: Intron
+Macromolecule #34: U6 snRNA
+Macromolecule #35: INOSITOL HEXAKISPHOSPHATE
+Macromolecule #36: GUANOSINE-5'-TRIPHOSPHATE
+Macromolecule #37: MAGNESIUM ION
+Macromolecule #38: 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 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.25 µm / Nominal defocus min: 1.25 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
Movie
Controller
About Yorodumi




Keywords
Homo sapiens (human)
Authors
France,
Austria, 5 items
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Z (Sec.)
Y (Row.)
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Processing
FIELD EMISSION GUN
