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Open data
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Basic information
| Entry | Database: PDB / ID: 9jns | ||||||||||||
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| Title | 50S precursor - Erm complex (C-II) | ||||||||||||
Components |
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Keywords | RIBOSOME / 50S precursor / Erm / methyltransferase / antibiotic resistance / ribosome-protein complex | ||||||||||||
| Function / homology | Function and homology information23S rRNA (adenine2085-N6)-dimethyltransferase / 23S rRNA (adenine(2085)-N(6))-dimethyltransferase activity / rRNA (adenine-N6,N6-)-dimethyltransferase activity / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / negative regulation of cytoplasmic translation / translation repressor activity / mRNA regulatory element binding translation repressor activity / assembly of large subunit precursor of preribosome ...23S rRNA (adenine2085-N6)-dimethyltransferase / 23S rRNA (adenine(2085)-N(6))-dimethyltransferase activity / rRNA (adenine-N6,N6-)-dimethyltransferase activity / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / negative regulation of cytoplasmic translation / translation repressor activity / mRNA regulatory element binding translation repressor activity / assembly of large subunit precursor of preribosome / ribosome assembly / cytosolic ribosome assembly / response to reactive oxygen species / DNA-templated transcription termination / response to radiation / mRNA 5'-UTR binding / large ribosomal subunit / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / response to antibiotic / negative regulation of DNA-templated transcription / mRNA binding / DNA binding / RNA binding / zinc ion binding / cytoplasm / cytosol Similarity search - Function | ||||||||||||
| Biological species | ![]() ![]() | ||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.7 Å | ||||||||||||
Authors | Sengupta, S. / Mukherjee, R. / Pilsl, M. / Bagale, S. / Adhikary, A.D. / Borkar, A. / Pradeepkumar, P.I. / Engel, C. / Chowdhury, A. / Kaushal, P.S. / Anand, R. | ||||||||||||
| Funding support | United Kingdom, India, 3items
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Citation | Journal: To Be PublishedTitle: Mechanistic Insights into 50S Precursor Recognition and Targeting by Erythromycin Resistance Methyltransferase Authors: Sengupta, S. / Mukherjee, R. / Pilsl, M. / Bagale, S. / Adhikary, A.D. / Borkar, A. / Pradeepkumar, P.I. / Engel, C. / Chowdhury, A. / Kaushal, P.S. / Anand, R. | ||||||||||||
| 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 | 9jns.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9jns.ent.gz | 864.9 KB | Display | PDB format |
| PDBx/mmJSON format | 9jns.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9jns_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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| Full document | 9jns_full_validation.pdf.gz | 1.4 MB | Display | |
| Data in XML | 9jns_validation.xml.gz | 86.5 KB | Display | |
| Data in CIF | 9jns_validation.cif.gz | 148 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jn/9jns ftp://data.pdbj.org/pub/pdb/validation_reports/jn/9jns | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 61625MC ![]() 9jmkC ![]() 9jsrC 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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| 1 |
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Components
-50S ribosomal protein ... , 16 types, 16 molecules 02DEJKLNPQRSTUYZ
| #1: Protein | Mass: 6463.445 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #2: Protein/peptide | Mass: 5397.463 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #5: Protein | Mass: 22277.535 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #6: Protein | Mass: 22121.566 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #7: Protein | Mass: 16050.606 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #8: Protein | Mass: 13565.067 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #9: Protein | Mass: 15008.471 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #10: Protein | Mass: 14393.657 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #11: Protein | Mass: 13159.278 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #12: Protein | Mass: 13528.024 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #13: Protein | Mass: 11586.374 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #14: Protein | Mass: 12253.359 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #15: Protein | Mass: 11222.160 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #16: Protein | Mass: 11339.250 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #17: Protein | Mass: 7286.464 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #18: Protein | Mass: 6554.820 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-RNA chain / Protein , 2 types, 2 molecules AC
| #3: RNA chain | Mass: 941612.375 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #4: Protein | Mass: 28955.529 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P13956, 23S rRNA (adenine2085-N6)-dimethyltransferase |
-Details
| Has protein modification | N |
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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: 50S precursor-Erm complex (C-1) / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
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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: 2500 nm / Nominal defocus min: 750 nm |
| Image recording | Electron dose: 41.25 e/Å2 / Film or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||
| 3D reconstruction | Resolution: 4.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 55608 / Symmetry type: POINT | ||||||||||||||||||||
| Atomic model building | Protocol: RIGID BODY FIT / Space: REAL |
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About Yorodumi






United Kingdom,
India, 3items
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FIELD EMISSION GUN