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Open data
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Basic information
| Entry | Database: PDB / ID: 9r8v | ||||||||||||||||||||||||
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| Title | Cryo-EM structure of the human pre-Bact-OTS complex (whole map) | ||||||||||||||||||||||||
Components |
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Keywords | SPLICING / spliceosome | ||||||||||||||||||||||||
| Function / homology | Function and homology informationprotein localization to P-body / DNA topoisomerase binding / RS domain binding / microfibril / Lsm2-8 complex / somatic diversification of immunoglobulins / U6 snRNA 3'-end binding / mRNA decay by 5' to 3' exoribonuclease / Lsm1-7-Pat1 complex / protein kinase B binding ...protein localization to P-body / DNA topoisomerase binding / RS domain binding / microfibril / Lsm2-8 complex / somatic diversification of immunoglobulins / U6 snRNA 3'-end binding / mRNA decay by 5' to 3' exoribonuclease / Lsm1-7-Pat1 complex / protein kinase B binding / U6 snRNP / PH domain binding / U11/U12 snRNP / regulation of retinoic acid receptor signaling pathway / interleukin-17-mediated signaling pathway / 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 / 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) / B-WICH complex / alternative mRNA splicing, via spliceosome / protein localization to kinetochore / protein methylation / 7-methylguanosine cap hypermethylation / U12-type spliceosomal complex / nuclear retinoic acid receptor binding / embryonic brain development / U1 snRNP binding / U2-type catalytic step 1 spliceosome / methylosome / pICln-Sm protein complex / ATP-dependent activity, acting on RNA / response to alkaloid / RNA splicing, via transesterification reactions / positive regulation of mRNA splicing, via spliceosome / signal transduction involved in regulation of gene expression / 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 / positive regulation of vitamin D receptor signaling pathway / snRNP binding / commitment complex / host-mediated activation of viral transcription / U2-type precatalytic spliceosome / mRNA cis splicing, via spliceosome / telomerase holoenzyme complex / Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells / RNA polymerase binding / Notch binding / RUNX3 regulates NOTCH signaling / telomerase RNA binding / U2-type prespliceosome assembly / U2-type catalytic step 2 spliceosome / Transport of Mature mRNA derived from an Intron-Containing Transcript / U2-type spliceosomal complex / nuclear vitamin D receptor binding / NOTCH4 Intracellular Domain Regulates Transcription / transcription elongation factor activity / U1 snRNP / SAGA complex / U2 snRNP / RNA Polymerase II Transcription Termination / U4 snRNP / P-body assembly / NOTCH3 Intracellular Domain Regulates Transcription / : / U2-type prespliceosome / tRNA processing / Basigin interactions / mRNA stabilization / positive regulation of transcription by RNA polymerase III / positive regulation of neurogenesis / nuclear androgen receptor binding / ubiquitin-ubiquitin ligase activity / precatalytic spliceosome / Notch-HLH transcription pathway / WW domain binding / ubiquitin-like protein conjugating enzyme binding / Formation of paraxial mesoderm / mitotic spindle assembly checkpoint signaling / WD40-repeat domain binding / regulation of alternative mRNA splicing, via spliceosome / mRNA 5'-splice site recognition / positive regulation of transforming growth factor beta receptor signaling pathway / mRNA 3'-splice site recognition / SMAD binding / regulation of RNA splicing / mRNA catabolic process Similarity search - Function | ||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 8.5 Å | ||||||||||||||||||||||||
Authors | Zhang, Z. / Kumar, V. / Zhong, J. / Dybkov, O. / Kastner, B. / Urlaub, H. / Luhrmann, R. | ||||||||||||||||||||||||
| Funding support | Germany, 1items
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Citation | Journal: To Be PublishedTitle: cryo-EM structure of the human pre-Bact-OTS complex Authors: Zhang, Z. / Kumar, V. / Dybkov, O. / Zhong, J. / Kastner, B. / Henning, U. / Luehrmann, R. | ||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9r8v.cif.gz | 2.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9r8v.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9r8v.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/r8/9r8v ftp://data.pdbj.org/pub/pdb/validation_reports/r8/9r8v | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 53843MC ![]() 9r3dC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
+Protein , 22 types, 25 molecules ALCGQRXqr2b5bBLSRDHxyvwtS1A6TKP75A
-U5 small nuclear ribonucleoprotein ... , 2 types, 2 molecules BE
| #2: Protein | Mass: 244823.422 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O75643, RNA helicase |
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| #9: Protein | Mass: 39359.492 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q96DI7 |
-RNA chain , 4 types, 4 molecules 265Z
| #3: RNA chain | Mass: 60186.445 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 36516 |
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| #4: RNA chain | Mass: 34098.270 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: NR_004394.1 |
| #6: RNA chain | Mass: 37254.855 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 20330981 |
| #37: RNA chain | Mass: 132594.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: PM5-10 pre-mRNA with MS2 loop / Source: (natural) Homo sapiens (human) |
-Splicing factor 3A subunit ... , 3 types, 3 molecules 798
| #5: Protein | Mass: 88991.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q15459 |
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| #27: Protein | Mass: 58934.844 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q12874 |
| #28: Protein | Mass: 49327.355 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q15428 |
-Pre-mRNA-splicing factor ... , 2 types, 2 molecules IP
| #11: Protein | Mass: 37563.863 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q8NAV1 |
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| #40: Protein | Mass: 56285.566 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
-Small nuclear ribonucleoprotein ... , 6 types, 12 molecules 22522f5f23532g5g2e5e2151
| #17: Protein | Mass: 13551.928 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62316#19: Protein | Mass: 9734.171 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62306#21: Protein | Mass: 13940.308 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62318#22: Protein | Mass: 8508.084 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62308#23: Protein | Mass: 10817.601 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62304#24: Protein | Mass: 13310.653 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62314 |
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-U2 small nuclear ribonucleoprotein ... , 2 types, 2 molecules 2B2A
| #18: Protein | Mass: 25524.367 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P08579 |
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| #25: Protein | Mass: 28456.584 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P09661 |
-Splicing factor 3B subunit ... , 6 types, 6 molecules B4B2B5B3B1B6
| #26: Protein | Mass: 44436.570 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q15427 |
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| #29: Protein | Mass: 100377.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q13435 |
| #30: Protein | Mass: 10149.369 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BWJ5 |
| #31: Protein | Mass: 135718.844 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q15393 |
| #32: Protein | Mass: 146024.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O75533 |
| #33: Protein | Mass: 14606.900 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y3B4 |
-U6 snRNA-associated Sm-like protein ... , 7 types, 7 molecules 62636465666768
| #42: Protein | Mass: 10847.495 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y333 |
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| #43: Protein | Mass: 11859.390 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62310 |
| #44: Protein | Mass: 15375.775 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y4Z0 |
| #45: Protein | Mass: 9945.448 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9Y4Y9 |
| #46: Protein | Mass: 9139.571 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62312 |
| #47: Protein | Mass: 11617.363 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9UK45 |
| #48: Protein | Mass: 10410.589 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95777 |
-Details
| Has protein modification | N |
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-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: OTS-stalled spliceosome complex / Type: COMPLEX / Entity ID: all / Source: NATURAL |
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| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.9 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: OTS-stalled spliceosome complex particles |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Microscopy | Model: TFS TITAN THEMIS |
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| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3500 nm / Nominal defocus min: 1500 nm |
| Image recording | Electron dose: 39 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||
| 3D reconstruction | Resolution: 8.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 55345 / Symmetry type: POINT |
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About Yorodumi




Homo sapiens (human)
Germany, 1items
Citation


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FIELD EMISSION GUN