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Yorodumi- PDB-3hoz: Complete RNA polymerase II elongation complex IV with a T-U misma... -
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- Basic information
Basic information
| Entry | Database: PDB / ID: 3hoz | ||||||
|---|---|---|---|---|---|---|---|
| Title | Complete RNA polymerase II elongation complex IV with a T-U mismatch and a frayed RNA 3'-guanine | ||||||
|  Components | 
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|  Keywords | TRANSCRIPTION / TRANSFERASE/DNA/RNA HYBRID / RNA-FRAYING / RNA POLYMERASE II / METAL BINDING / TRANSCRIPTION BUBBLE / ELONGATION COMPLEX / DNA-RNA MISMATCH / RNA fraying / DNA-binding / DNA-directed RNA polymerase / Isopeptide bond / Magnesium / Nucleotidyltransferase / Nucleus / Phosphoprotein / Transferase / Ubl conjugation / Zinc / Zinc-finger / Polymorphism / Cytoplasm / DNA damage / DNA repair / mRNA processing / TRANSFERASE-DNA-RNA HYBRID COMPLEX | ||||||
| Function / homology |  Function and homology information RPB4-RPB7 complex / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / 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 ...RPB4-RPB7 complex / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / 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 / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / 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 / Estrogen-dependent gene expression / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / nuclear-transcribed mRNA catabolic process / transcription by RNA polymerase III / positive regulation of translational initiation / Dual incision in TC-NER / 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 / translation initiation factor binding / transcription-coupled nucleotide-excision repair / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / P-body / DNA-templated transcription initiation / ribonucleoside binding / mRNA processing / DNA-directed RNA polymerase / cytoplasmic stress granule / DNA-directed RNA polymerase activity / peroxisome / ribosome biogenesis / single-stranded DNA binding / nucleic acid binding / transcription by RNA polymerase II / single-stranded RNA binding / protein dimerization activity / nucleotide binding / mRNA binding / nucleolus / mitochondrion / DNA binding / zinc ion binding / nucleoplasm / metal ion binding / nucleus / cytoplasm Similarity search - Function | ||||||
| Biological species |   Saccharomyces cerevisiae (brewer's yeast) | ||||||
| Method |  X-RAY DIFFRACTION /  SYNCHROTRON /  MOLECULAR REPLACEMENT / Resolution: 3.65 Å | ||||||
|  Authors | Sydow, J.F. / Brueckner, F. / Cheung, A.C.M. / Damsma, G.E. / Dengl, S. / Lehmann, E. / Vassylyev, D. / Cramer, P. | ||||||
|  Citation |  Journal: Mol.Cell / Year: 2009 Title: Structural basis of transcription: mismatch-specific fidelity mechanisms and paused RNA polymerase II with frayed RNA. Authors: Sydow, J.F. / Brueckner, F. / Cheung, A.C.M. / Damsma, G.E. / Dengl, S. / Lehmann, E. / Vassylyev, D. / 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 |  3hoz.cif.gz | 831 KB | Display |  PDBx/mmCIF format | 
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| PDB format |  pdb3hoz.ent.gz | 649.3 KB | Display |  PDB format | 
| PDBx/mmJSON format |  3hoz.json.gz | Tree view |  PDBx/mmJSON format | |
| Others |  Other downloads | 
-Validation report
| Summary document |  3hoz_validation.pdf.gz | 633.8 KB | Display |  wwPDB validaton report | 
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| Full document |  3hoz_full_validation.pdf.gz | 1004.6 KB | Display | |
| Data in XML |  3hoz_validation.xml.gz | 181.6 KB | Display | |
| Data in CIF |  3hoz_validation.cif.gz | 246.7 KB | Display | |
| Arichive directory |  https://data.pdbj.org/pub/pdb/validation_reports/ho/3hoz  ftp://data.pdbj.org/pub/pdb/validation_reports/ho/3hoz | HTTPS FTP | 
-Related structure data
| Related structure data |  3houSC  3hovC  3howC  3hoxC  3hoyC S: Starting model for refinement C: citing same article ( | 
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| Similar structure data | 
- Links
Links
- Assembly
Assembly
| Deposited unit |  
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| 1 | 
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| Unit cell | 
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- Components
Components
-DNA-directed RNA polymerase II subunit  ... , 7 types, 7 molecules ABCDGIK      
| #1: Protein | Mass: 191821.578 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P04050, DNA-directed RNA polymerase | 
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| #2: Protein | Mass: 138937.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P08518, DNA-directed RNA polymerase | 
| #3: Protein | Mass: 38677.918 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P16370, DNA-directed RNA polymerase | 
| #4: Protein | Mass: 25451.191 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P20433, DNA-directed RNA polymerase | 
| #7: Protein | Mass: 19081.053 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P34087, DNA-directed RNA polymerase | 
| #9: Protein | Mass: 14308.161 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P27999, DNA-directed RNA polymerase | 
| #11: Protein | Mass: 13633.493 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P38902, DNA-directed RNA polymerase | 
-DNA-directed RNA polymerases I, II, and III subunit  ... , 5 types, 5 molecules EFHJL    
| #5: Protein | Mass: 25117.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P20434, DNA-directed RNA polymerase | 
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| #6: Protein | Mass: 17931.834 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P20435, DNA-directed RNA polymerase | 
| #8: Protein | Mass: 16525.363 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P20436, DNA-directed RNA polymerase | 
| #10: Protein | Mass: 8290.732 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P22139, DNA-directed RNA polymerase | 
| #12: Protein | Mass: 7729.969 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)    Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P40422, DNA-directed RNA polymerase | 
-DNA chain , 2 types, 2 molecules NT 
| #13: DNA chain | Mass: 3637.391 Da / Num. of mol.: 1 / Source method: obtained synthetically | 
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| #14: DNA chain | Mass: 8034.007 Da / Num. of mol.: 1 / Source method: obtained synthetically | 
-RNA chain , 1 types, 1 molecules P
| #15: RNA chain | Mass: 5709.428 Da / Num. of mol.: 1 / Source method: obtained synthetically | 
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-Non-polymers , 2 types, 9 molecules 


| #16: Chemical | ChemComp-ZN / #17: Chemical | ChemComp-MG / |  | 
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-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
Sample preparation
| Crystal | Density Matthews: 5.74 Å3/Da / Density % sol: 78.58 % | 
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 20mM ammonium acetate, 300mM SODIUM ACETATE, 50mM Hepes pH 7.0, 4-6% PEG 6000, 5mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 293K | 
-Data collection
| Diffraction | Mean temperature: 100 K | 
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| Diffraction source | Source:  SYNCHROTRON / Site:  SLS  / Beamline: X06SA / Wavelength: 0.9188 Å | 
| Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Mar 17, 2008 | 
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | 
| Radiation wavelength | Wavelength: 0.9188 Å / Relative weight: 1 | 
| Reflection | Resolution: 3.65→50 Å / Num. all: 135977 / Num. obs: 135977 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.6 % / Rsym value: 0.077 / Net I/σ(I): 22 | 
- Processing
Processing
| Software | 
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| Refinement | Method to determine structure:  MOLECULAR REPLACEMENT Starting model: 3HOU Resolution: 3.65→50 Å / Isotropic thermal model: isotropic / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber 
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| Refinement step | Cycle: LAST / Resolution: 3.65→50 Å 
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