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Open data
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Basic information
| Entry | Database: PDB / ID: 1y1y | ||||||
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| Title | RNA Polymerase II-TFIIS-DNA/RNA complex | ||||||
Components |
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Keywords | TRANSFERASE/TRANSCRIPTION/DNA-RNA HYBRID / RNA Polymerase II / TFIIS / nucleic acids / transcription / readthrough / TRANSFERASE-TRANSCRIPTION-DNA-RNA HYBRID COMPLEX | ||||||
| Function / homology | Function and homology information: / regulation of mRNA 3'-end processing / RPB4-RPB7 complex / transcription elongation factor activity / 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 ...: / regulation of mRNA 3'-end processing / RPB4-RPB7 complex / transcription elongation factor activity / 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 / Formation of TC-NER Pre-Incision Complex / Estrogen-dependent gene expression / RNA polymerase II transcribes snRNA genes / RNA Polymerase I Promoter Escape / 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 / RNA Polymerase II Pre-transcription Events / RNA-templated transcription / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / termination of RNA polymerase II transcription / RNA polymerase II complex binding / Gap-filling DNA repair synthesis and ligation in TC-NER / termination of RNA polymerase I transcription / Dual incision in TC-NER / transcription by RNA polymerase III / positive regulation of RNA polymerase II transcription preinitiation complex assembly / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / nucleolar large rRNA transcription by RNA polymerase I / transcription initiation at RNA polymerase I promoter / positive regulation of translational initiation / nuclear-transcribed mRNA catabolic process / termination of RNA polymerase III transcription / transcription initiation at RNA polymerase III promoter / RNA polymerase I complex / RNA polymerase III complex / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / transcription by RNA polymerase I / transcription elongation by RNA polymerase I / translesion synthesis / transcription-coupled nucleotide-excision repair / translation initiation factor binding / RNA polymerase II transcription regulatory region sequence-specific DNA binding / transcription antitermination / positive regulation of transcription elongation by RNA polymerase II / DNA-templated transcription initiation / transcription initiation at RNA polymerase II promoter / P-body / transcription elongation by RNA polymerase II / mRNA transcription by RNA polymerase II / ribonucleoside binding / mRNA processing / cytoplasmic stress granule / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / transcription by RNA polymerase II / peroxisome / single-stranded DNA binding / ribosome biogenesis / nucleic acid binding / protein dimerization activity / single-stranded RNA binding / nucleotide binding / mRNA binding / nucleolus / mitochondrion / DNA binding / nucleoplasm / zinc ion binding / metal ion binding / nucleus / cytoplasm Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4 Å | ||||||
Authors | Cramer, P. / Kettenberger, H. / Armache, K.-J. | ||||||
Citation | Journal: Mol.Cell / Year: 2004Title: Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS. Authors: Kettenberger, H. / Armache, K.J. / Cramer, P. | ||||||
| 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 | 1y1y.cif.gz | 179.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1y1y.ent.gz | 99.7 KB | Display | PDB format |
| PDBx/mmJSON format | 1y1y.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y1/1y1y ftp://data.pdbj.org/pub/pdb/validation_reports/y1/1y1y | HTTPS FTP |
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-Related structure data
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Unit cell |
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Components
-DNA-directed RNA polymerase II ... , 7 types, 7 molecules ABCDGIK
| #3: Protein | Mass: 191821.578 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #4: Protein | Mass: 138937.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #5: Protein | Mass: 35330.457 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #6: Protein | Mass: 25451.191 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein | Mass: 19081.053 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #11: Protein | Mass: 14308.161 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #13: Protein | Mass: 13633.493 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-DNA-directed RNA polymerases I, II, and III ... , 4 types, 4 molecules EFHL
| #7: Protein | Mass: 25117.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #8: Protein | Mass: 17931.834 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 16525.363 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #14: Protein | Mass: 7729.969 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 2 types, 2 molecules JS
| #12: Protein | Mass: 8290.732 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #15: Protein | Mass: 20271.938 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: DST1 / Plasmid: pET28A / Production host: ![]() |
-DNA chain / RNA chain , 2 types, 2 molecules TP
| #1: DNA chain | Mass: 2073.386 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: synthetic oligonucleotide |
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| #2: RNA chain | Mass: 1279.842 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: synthetic oligonucleotide |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 5.71 Å3/Da / Density % sol: 78.47 % |
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-Data collection
| Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.9919 Å |
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| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.9919 Å / Relative weight: 1 |
| Reflection | Resolution: 4→50 Å / Num. all: 103460 / Num. obs: 103460 / % possible obs: 98.7 % / Observed criterion σ(F): 20.3 / Observed criterion σ(I): 20.3 / Redundancy: 4.3 % / Rsym value: 0.07 |
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Processing
| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 4→50 Å / σ(F): 5.4 / Stereochemistry target values: Engh & HuberDetails: The coordinates for only the alpha carbons and phosphorus atoms are present in the structure. The number of missing atoms was so much that remark 470 for the missing atoms list were removed.
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| Refinement step | Cycle: LAST / Resolution: 4→50 Å
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