+ Open data
Open data
- Basic information
Basic information
| Entry | Database: PDB / ID: 9g0a | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Title | Influenza A/H7N9 polymerase post-cleavage cap-snatching complex | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|  Components | 
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|  Keywords | VIRUS / Influenza virus / influenza A / cap-snatching / transcription | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Function / homology |  Function and homology information negative regulation of DNA-templated transcription, elongation / DSIF complex / regulation of transcription elongation by RNA polymerase II / Formation of RNA Pol II elongation complex  / Formation of the Early Elongation Complex / Transcriptional regulation by small RNAs / RNA Polymerase II Pre-transcription Events / TP53 Regulates Transcription of DNA Repair Genes / FGFR2 alternative splicing / RNA polymerase II transcribes snRNA genes ...negative regulation of DNA-templated transcription, elongation / DSIF complex / regulation of transcription elongation by RNA polymerase II / Formation of RNA Pol II elongation complex  / Formation of the Early Elongation Complex / Transcriptional regulation by small RNAs / RNA Polymerase II Pre-transcription Events / TP53 Regulates Transcription of DNA Repair Genes / FGFR2 alternative splicing / RNA polymerase II transcribes snRNA genes / mRNA Capping / mRNA Splicing - Minor Pathway / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Elongation / RNA Polymerase II Transcription Initiation And Promoter Clearance / RNA Pol II CTD phosphorylation and interaction with CE / Estrogen-dependent gene expression / Formation of TC-NER Pre-Incision Complex / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / mRNA Splicing - Major Pathway / positive regulation of DNA-templated transcription, elongation / Abortive elongation of HIV-1 transcript in the absence of Tat / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / transcription elongation-coupled chromatin remodeling / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / cap snatching / mRNA Capping / viral transcription / RNA polymerase II complex binding / symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / negative regulation of transcription elongation by RNA polymerase II / positive regulation of macroautophagy / RNA polymerase II transcribes snRNA genes / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / 7-methylguanosine mRNA capping / host cell mitochondrion / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / RNA polymerase I complex / transcription elongation by RNA polymerase I / RNA polymerase III complex / core promoter sequence-specific DNA binding / Formation of HIV elongation complex in the absence of HIV Tat / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / transcription by RNA polymerase I / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex  / translation initiation factor binding / transcription-coupled nucleotide-excision repair / RNA Polymerase II Pre-transcription Events / DNA-directed RNA polymerase complex / TP53 Regulates Transcription of DNA Repair Genes / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / DNA-templated transcription initiation / positive regulation of transcription elongation by RNA polymerase II / euchromatin / virion component / ribonucleoside binding / fibrillar center / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / endonuclease activity / nucleic acid binding / Hydrolases; Acting on ester bonds / transcription by RNA polymerase II / host cell cytoplasm / protein dimerization activity / nuclear speck / symbiont-mediated suppression of host gene expression / protein heterodimerization activity / viral translational frameshifting / RNA-directed RNA polymerase / viral RNA genome replication / nucleotide binding / RNA-directed RNA polymerase activity / mRNA binding / DNA-templated transcription / chromatin binding / regulation of DNA-templated transcription / nucleolus / host cell nucleus / enzyme binding / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / mitochondrion / DNA binding / RNA binding / zinc ion binding Similarity search - Function | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Biological species |  Homo sapiens (human)   Influenza A virus   Sus scrofa domesticus (domestic pig)  Influenza B virus synthetic construct (others) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|  Authors | Rotsch, A.H. / Li, D. / Dienemann, C. / Cusack, S. / Cramer, P. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Funding support |  Germany, European Union, 2items 
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|  Citation |  Journal: To Be Published Title: Mechanism of Co-Transcriptional Cap-Snatching by Influenza Polymerase Authors: Rotsch, A.H. / Li, D. / Dupont, M. / Krischuns, T. / Oberthuer, C. / Stelfox, A. / Lukarska, M. / Fianu, I. / Lidschreiber, M. / Naffakh, N. / Dienemann, C. / Cusack, S. / Cramer, P. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| History | 
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- Structure visualization
Structure visualization
| Structure viewer | Molecule:  Molmil  Jmol/JSmol | 
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- Downloads & links
Downloads & links
- Download
Download
| PDBx/mmCIF format |  9g0a.cif.gz | 1.5 MB | Display |  PDBx/mmCIF format | 
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| PDB format |  pdb9g0a.ent.gz | 1.1 MB | Display |  PDB format | 
| PDBx/mmJSON format |  9g0a.json.gz | Tree view |  PDBx/mmJSON format | |
| Others |  Other downloads | 
-Validation report
| Summary document |  9g0a_validation.pdf.gz | 1.6 MB | Display |  wwPDB validaton report | 
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| Full document |  9g0a_full_validation.pdf.gz | 1.8 MB | Display | |
| Data in XML |  9g0a_validation.xml.gz | 182.2 KB | Display | |
| Data in CIF |  9g0a_validation.cif.gz | 292.5 KB | Display | |
| Arichive directory |  https://data.pdbj.org/pub/pdb/validation_reports/g0/9g0a  ftp://data.pdbj.org/pub/pdb/validation_reports/g0/9g0a | HTTPS FTP | 
-Related structure data
| Related structure data |  50927MC  9fyxC C: citing same article ( M: map data used to model this data | 
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| Similar structure data | Similarity search - Function & homology  F&H Search | 
- Links
Links
- Assembly
Assembly
| Deposited unit |  
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| 1 | 
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- Components
Components
-Transcription elongation factor  ... , 2 types, 2 molecules ZY 
| #1: Protein | Mass: 121145.477 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Homo sapiens (human) / Gene: SUPT5H, SPT5, SPT5H / Production host:   Escherichia coli (E. coli) / References: UniProt: O00267 | 
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| #2: Protein | Mass: 13210.201 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Homo sapiens (human) / Gene: SUPT4H1, SPT4H, SUPT4H / Production host:   Escherichia coli (E. coli) / References: UniProt: P63272 | 
-DNA-directed RNA polymerase  ... , 7 types, 7 molecules ABCEIKG      
| #3: Protein | Mass: 183244.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Sus scrofa domesticus (domestic pig) / References: UniProt: I3LJR4, DNA-directed RNA polymerase | 
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| #11: Protein | Mass: 134041.422 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Sus scrofa domesticus (domestic pig) References: UniProt: A0A0B8RVL1, DNA-directed RNA polymerase | 
| #12: Protein | Mass: 31439.074 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Sus scrofa domesticus (domestic pig) / References: UniProt: I3LCH3 | 
| #13: Protein | Mass: 24644.318 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Sus scrofa domesticus (domestic pig) / References: UniProt: I3LSI7 | 
| #16: Protein | Mass: 14541.221 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Sus scrofa domesticus (domestic pig) / References: UniProt: P60899 | 
| #18: Protein | Mass: 13310.284 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Sus scrofa domesticus (domestic pig) / References: UniProt: F1RKE4 | 
| #23: Protein | Mass: 19314.283 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Sus scrofa domesticus (domestic pig) / References: UniProt: A0A4X1VKG7 | 
-RNA chain , 3 types, 3 molecules Prv  
| #4: RNA chain | Mass: 11437.029 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.)   Influenza B virus | 
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| #8: RNA chain | Mass: 4008.358 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.)   Influenza B virus | 
| #9: RNA chain | Mass: 4557.820 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.)   Influenza B virus | 
-Protein , 3 types, 3 molecules abc  
| #5: Protein | Mass: 82916.570 Da / Num. of mol.: 1 / Mutation: E119D Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9)) Gene: PA / Production host:  Trichoplusia ni (cabbage looper) References: UniProt: M9TI86, Hydrolases; Acting on ester bonds | 
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| #6: Protein | Mass: 86496.156 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9)) Gene: PB1 / Production host:  Trichoplusia ni (cabbage looper) / References: UniProt: M9TLW3, RNA-directed RNA polymerase | 
| #7: Protein | Mass: 86007.320 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9)) Gene: PB2 / Production host:  Trichoplusia ni (cabbage looper) / References: UniProt: X5F427 | 
-Protein/peptide , 1 types, 1 molecules X
| #10: Protein/peptide | Mass: 1089.200 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: register is based on first phenylalanine in linker / Source: (gene. exp.)  Homo sapiens (human) / Production host:   Escherichia coli (E. coli) | 
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-DNA-directed RNA polymerases I, II, and III subunit  ... , 3 types, 3 molecules FHJ  
| #14: Protein | Mass: 14477.001 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Sus scrofa domesticus (domestic pig) / References: UniProt: A0A4X1VEK9 | 
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| #15: Protein | Mass: 17162.273 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Sus scrofa domesticus (domestic pig) / References: UniProt: I3LCB2 | 
| #17: Protein | Mass: 7655.123 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Sus scrofa domesticus (domestic pig) / References: UniProt: A0A4X1VYD0 | 
-RNA polymerase  ... , 2 types, 2 molecules LD 
| #19: Protein | Mass: 7018.244 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Sus scrofa domesticus (domestic pig) / References: UniProt: A0A4X1TRS6 | 
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| #22: Protein | Mass: 20962.621 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Sus scrofa domesticus (domestic pig) / References: UniProt: A0A287ADR4 | 
-DNA chain , 2 types, 2 molecules NT 
| #20: DNA chain | Mass: 13303.563 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) | 
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| #21: DNA chain | Mass: 13193.495 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) | 
-Non-polymers , 4 types, 14 molecules 






| #24: Chemical | ChemComp-ZN / #25: Chemical | #26: Chemical | ChemComp-G1G / | #27: Chemical |  | 
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-Details
| Has ligand of interest | Y | 
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| Has protein modification | Y | 
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY | 
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction | 
- Sample preparation
Sample preparation
| Component | 
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| Molecular weight | Experimental value: NO | ||||||||||||||||||||||||||||||||||||||||||
| Source (natural) | 
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| Source (recombinant) | 
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| Buffer solution | pH: 8 Details: 20 mM BICINE pH 8.0 150 mM NaCl 3 mM MgCl2 4% glycerol | ||||||||||||||||||||||||||||||||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 95 % | 
- Electron microscopy imaging
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: OTHER | 
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 200 nm | 
| Image recording | Average exposure time: 2.4 sec. / Electron dose: 40 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) | 
- Processing
Processing
| EM software | 
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 11935228 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 63230 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement | Cross valid method: NONE | 
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