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Open data
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Basic information
| Entry | Database: PDB / ID: 3gtm | |||||||||
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| Title | Co-complex of Backtracked RNA polymerase II with TFIIS | |||||||||
Components |
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Keywords | TRANSCRIPTION / TRANSFERASE/DNA-RNA HYBRID / TRANSFERASE / DNA-RNA HYBRID / Backtrack / DNA-directed RNA polymerase / DNA binding / Isopeptide bond / Magnesium / Metal binding / Nucleotidyltransferase / Nucleus / Phosphoprotein / Ubl conjugation / Zinc / Zinc-finger / Polymorphism / Cytoplasm / DNA damage / DNA repair / Transcription regulation / TRANSFERASE-DNA-RNA HYBRID COMPLEX | |||||||||
| Function / homology | Function and homology informationRNA polymerase II complex recruiting activity / regulation of mRNA 3'-end processing / RNA Polymerase I Transcription Initiation / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / mRNA Capping / RNA polymerase II transcribes snRNA genes / termination of RNA polymerase II transcription ...RNA polymerase II complex recruiting activity / regulation of mRNA 3'-end processing / RNA Polymerase I Transcription Initiation / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / mRNA Capping / RNA polymerase II transcribes snRNA genes / termination of RNA polymerase II transcription / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Initiation And Promoter Clearance / termination of RNA polymerase III transcription / RNA Polymerase II Pre-transcription Events / RNA-templated transcription / Formation of TC-NER Pre-Incision Complex / transcription initiation at RNA polymerase III promoter / RNA Polymerase I Promoter Escape / termination of RNA polymerase I transcription / nucleolar large rRNA transcription by RNA polymerase I / Gap-filling DNA repair synthesis and ligation in TC-NER / transcription initiation at RNA polymerase I promoter / RNA polymerase II complex binding / Estrogen-dependent gene expression / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / transcription by RNA polymerase III / Dual incision in TC-NER / positive regulation of RNA polymerase II transcription preinitiation complex assembly / translesion synthesis / RNA polymerase I complex / transcription elongation by RNA polymerase I / RNA polymerase III complex / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / transcription by RNA polymerase I / transcription-coupled nucleotide-excision repair / transcription antitermination / RNA polymerase II transcription regulatory region sequence-specific DNA binding / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / positive regulation of transcription elongation by RNA polymerase II / ribonucleoside binding / DNA-directed RNA polymerase / cytoplasmic stress granule / DNA-directed RNA polymerase activity / peroxisome / ribosome biogenesis / nucleic acid binding / transcription by RNA polymerase II / protein dimerization activity / mRNA binding / regulation of transcription by RNA polymerase II / nucleolus / mitochondrion / DNA binding / zinc ion binding / nucleoplasm / metal ion binding / nucleus / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() synthetic construct (others) | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.8 Å | |||||||||
Authors | Wang, D. / Bushnell, D.A. / Huang, X. / Westover, K.D. / Levitt, M. / Kornberg, R.D. | |||||||||
Citation | Journal: Science / Year: 2009Title: Structural basis of transcription: backtracked RNA polymerase II at 3.4 angstrom resolution. Authors: Wang, D. / Bushnell, D.A. / Huang, X. / Westover, K.D. / Levitt, M. / Kornberg, R.D. | |||||||||
| History |
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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 | 3gtm.cif.gz | 1.5 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb3gtm.ent.gz | 1.2 MB | Display | PDB format |
| PDBx/mmJSON format | 3gtm.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 3gtm_validation.pdf.gz | 595.2 KB | Display | wwPDB validaton report |
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| Full document | 3gtm_full_validation.pdf.gz | 752.5 KB | Display | |
| Data in XML | 3gtm_validation.xml.gz | 142.7 KB | Display | |
| Data in CIF | 3gtm_validation.cif.gz | 192.9 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gt/3gtm ftp://data.pdbj.org/pub/pdb/validation_reports/gt/3gtm | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 3gtgC ![]() 3gtjC ![]() 3gtkC ![]() 3gtlC ![]() 3gtoC ![]() 3gtpC ![]() 3gtqC ![]() 1y1vS C: citing same article ( S: Starting model for refinement |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| Unit cell |
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| Details | ASYMMETRIC UNIT IS THE BIOLOGICAL UNIT |
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Components
-DNA-directed RNA polymerase II subunit ... , 5 types, 5 molecules ABCIK
| #1: Protein | Mass: 191821.578 Da / Num. of mol.: 1 / Fragment: DNA-directed RNA polymerase II largest subunit / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P04050, DNA-directed RNA polymerase |
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| #2: Protein | Mass: 138937.297 Da / Num. of mol.: 1 Fragment: DNA-directed RNA polymerase II 140 kDa polypeptide Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P08518, DNA-directed RNA polymerase |
| #3: Protein | Mass: 35330.457 Da / Num. of mol.: 1 / Fragment: DNA-directed RNA polymerase II 45 kDa polypeptide / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P16370 |
| #7: Protein | Mass: 14308.161 Da / Num. of mol.: 1 / Fragment: DNA-directed RNA polymerase II subunit 9 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P27999 |
| #9: Protein | Mass: 13633.493 Da / Num. of mol.: 1 Fragment: DNA-directed RNA polymerase II 13.6 kDa polypeptide Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P38902 |
-DNA-directed RNA polymerases I, II, and III subunit ... , 5 types, 5 molecules EFHJL
| #4: Protein | Mass: 25117.094 Da / Num. of mol.: 1 Fragment: DNA-directed RNA polymerases I, II, and III 27 kDa polypeptide Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P20434 |
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| #5: Protein | Mass: 17931.834 Da / Num. of mol.: 1 Fragment: DNA-directed RNA polymerases I, II, and III 23 kDa polypeptide Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P20435 |
| #6: Protein | Mass: 16525.363 Da / Num. of mol.: 1 Fragment: DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P20436 |
| #8: Protein | Mass: 8290.732 Da / Num. of mol.: 1 / Fragment: DNA-directed RNA polymerases I/II/III subunit 10 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P22139 |
| #10: Protein | Mass: 7729.969 Da / Num. of mol.: 1 Fragment: DNA-directed RNA polymerases I, II, and III 7.7 kDa polypeptide Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P40422 |
-DNA chain , 2 types, 2 molecules NO
| #13: DNA chain | Mass: 8534.519 Da / Num. of mol.: 1 / Fragment: DNA template strand / Source method: obtained synthetically / Details: Synthetic template DNA / Source: (synth.) synthetic construct (others) |
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| #14: DNA chain | Mass: 4286.789 Da / Num. of mol.: 1 / Fragment: DNA non-template strand / Source method: obtained synthetically / Details: Synthetic non-template DNA / Source: (synth.) synthetic construct (others) |
-Protein / RNA chain , 2 types, 2 molecules SM
| #11: Protein | Mass: 19732.430 Da / Num. of mol.: 1 Fragment: Transcription Factor IIS E291H mutation, UNP residues 147-309 Mutation: E291H Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 204508 / S288c / Gene: DST1, PPR2, YGL043W / Production host: ![]() |
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| #12: RNA chain | Mass: 4220.589 Da / Num. of mol.: 1 / Fragment: RNA strand / Source method: obtained synthetically / Details: Synthetic RNA / Source: (synth.) synthetic construct (others) |
-Non-polymers , 2 types, 10 molecules 


| #15: Chemical | ChemComp-MG / |
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| #16: Chemical | ChemComp-ZN / |
-Details
| Has protein modification | Y |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.55 Å3/Da / Density % sol: 65.32 % | ||||||||||||||||||||||||||||||||||||
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| Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 390mM (NH4)2HPO4/NaH2PO4, pH 6.0, 50mM Dioxane, 10mM DTT, 9-11% PEG 6000, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||||||||
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-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 0.98 Å |
| Detector | Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Mar 24, 2007 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
| Reflection | Resolution: 3.8→40 Å / Num. obs: 65617 / % possible obs: 94.8 % / Redundancy: 2 % / Net I/σ(I): 5.4 |
| Reflection shell | Resolution: 3.8→3.9 Å / Redundancy: 1.9 % / Mean I/σ(I) obs: 1.7 / % possible all: 94.2 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB entry 1Y1V Resolution: 3.8→40 Å
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| Refinement step | Cycle: LAST / Resolution: 3.8→40 Å
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| Refinement TLS params. | Refine-ID: X-RAY DIFFRACTION
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| Refinement TLS group |
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