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Yorodumi- PDB-28rf: Cryo-EM single particle structure of the Plastid-Encoded RNA Poly... -
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Basic information
| Entry | Database: PDB / ID: 28rf | |||||||||
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| Title | Cryo-EM single particle structure of the Plastid-Encoded RNA Polymerase (PEP)from Chlamydomonas reinhardtii. | |||||||||
Components |
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Keywords | RNA / Chlamydomonas reinhardtii / Plastid-Encoded RNA / Polymerase / Cryo-EM | |||||||||
| Function / homology | Function and homology informationlipid X metabolic process / plastid-encoded plastid RNA polymerase complex / carboxylic acid biosynthetic process / acid-amino acid ligase activity / glucose-6-phosphate 1-epimerase activity / UDP-3-O-acyl-N-acetylglucosamine deacetylase / UDP-3-O-acyl-N-acetylglucosamine deacetylase activity / ligase activity / lipid A biosynthetic process / catalytic activity ...lipid X metabolic process / plastid-encoded plastid RNA polymerase complex / carboxylic acid biosynthetic process / acid-amino acid ligase activity / glucose-6-phosphate 1-epimerase activity / UDP-3-O-acyl-N-acetylglucosamine deacetylase / UDP-3-O-acyl-N-acetylglucosamine deacetylase activity / ligase activity / lipid A biosynthetic process / catalytic activity / RNA processing / mitochondrion organization / chloroplast / ribonucleoside binding / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / carbohydrate binding / carbohydrate metabolic process / DNA-templated transcription / metal ion binding / DNA binding / RNA binding / zinc ion binding / ATP binding Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.65 Å | |||||||||
Authors | Kumar, A. / Schuller, S. / Schuller, J. | |||||||||
| Funding support | European Union, 1items
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Citation | Journal: To Be PublishedTitle: Cryo-EM single particle structure of the Plastid-Encoded RNA Polymerase (PEP)from Chlamydomonas reinhardtii. Authors: Schuller, S. / Kumar, A. / Schuller, J. | |||||||||
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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 | 28rf.cif.gz | 2.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb28rf.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 28rf.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/8r/28rf ftp://data.pdbj.org/pub/pdb/validation_reports/8r/28rf | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 56766MC ![]() 57515 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 , 8 types, 10 molecules AZFGHIKNQR
| #1: Protein | Mass: 83315.547 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: A0A218N9C3, DNA-directed RNA polymerase #6: Protein | | Mass: 69851.352 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | | Mass: 89099.086 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | Mass: 66248.688 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: A0A2K3CSZ9, UDP-3-O-acyl-N-acetylglucosamine deacetylase #10: Protein | | Mass: 280466.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | | Mass: 86417.430 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein | | Mass: 43963.891 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein | | Mass: 40289.797 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-DNA-directed RNA polymerase ... , 4 types, 4 molecules BCDE
| #2: Protein | Mass: 93313.695 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #3: Protein | Mass: 70525.086 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #4: Protein | Mass: 358327.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #5: Protein | Mass: 221076.719 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: A0A218N8D6, DNA-directed RNA polymerase |
-Uncharacterized ... , 5 types, 6 molecules JMSTXY
| #9: Protein | Mass: 38135.762 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #11: Protein | Mass: 189894.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #15: Protein | Mass: 41104.062 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #16: Protein | Mass: 40748.148 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #17: Protein | Mass: 44891.465 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Details
| Has protein modification | Y |
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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: Plastid-Encoded RNA Polymerase (PEP) from Chlamydomonas reinhardtii Type: COMPLEX / Entity ID: all / Source: NATURAL |
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| Molecular weight | Value: 2 MDa / Experimental value: YES |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 500 nm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.65 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 650394 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 2.65 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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FIELD EMISSION GUN