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Yorodumi- PDB-9i88: Structure of the wild-type Staphylococcus aureus 70S ribosome com... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9i88 | |||||||||||||||||||||||||||
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| Title | Structure of the wild-type Staphylococcus aureus 70S ribosome complexed with clincelin | |||||||||||||||||||||||||||
Components |
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Keywords | RIBOSOME / Antibiotic / Translation / Clincelin / Protein synthesis inhibitor / Staphylococcus aureus | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationlarge ribosomal subunit / ribosomal small subunit assembly / transferase activity / ribosome biogenesis / ribosomal small subunit biogenesis / 5S rRNA binding / small ribosomal subunit / ribosomal large subunit assembly / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit ...large ribosomal subunit / ribosomal small subunit assembly / transferase activity / ribosome biogenesis / ribosomal small subunit biogenesis / 5S rRNA binding / small ribosomal subunit / ribosomal large subunit assembly / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / RNA binding / zinc ion binding / cytoplasm / cytosol Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.98 Å | |||||||||||||||||||||||||||
Authors | Novotna, M. / Boissier, F. / Balikova Novotna, G. / Innis, C.A. | |||||||||||||||||||||||||||
| Funding support | Czech Republic, France, 4items
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Citation | Journal: To Be PublishedTitle: Structure of the wild-type Staphylococcus aureus 70S ribosome complexed with clincelin Authors: Novotna, M. / Slavik, P. / Demay, F. / Mahor, D. / Reha, D. / Boissier, F. / Pokorna, J. / Vimberg, V. / Brajerova, M. / Stefani, T. / Svoboda, J. / Gazak, R. / Marz, M. / Hosek, J. / ...Authors: Novotna, M. / Slavik, P. / Demay, F. / Mahor, D. / Reha, D. / Boissier, F. / Pokorna, J. / Vimberg, V. / Brajerova, M. / Stefani, T. / Svoboda, J. / Gazak, R. / Marz, M. / Hosek, J. / Koberska, M. / Eigner, V. / Hanzlikova, L. / Kuzma, M. / Krutova, M. / Kamenik, Z. / Sigut, K. / Janata, J. / Innis, C.A. / Balikova Novotna, G. | |||||||||||||||||||||||||||
| 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 | 9i88.cif.gz | 3.5 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9i88.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9i88.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i8/9i88 ftp://data.pdbj.org/pub/pdb/validation_reports/i8/9i88 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 52711MC 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
+Large ribosomal subunit protein ... , 27 types, 27 molecules 12356789GHIJKMNOPQRSTUVWXZ4
-RNA chain , 4 types, 4 molecules BDAa
| #9: RNA chain | Mass: 36974.945 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #10: RNA chain | Mass: 24788.754 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #49: RNA chain | Mass: 946697.625 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #50: RNA chain | Mass: 502058.344 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 1 types, 1 molecules Y
| #28: Protein | Mass: 23810.609 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Small ribosomal subunit protein ... , 19 types, 19 molecules cdefgijklmnopqrstuh
| #30: Protein | Mass: 29136.369 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #31: Protein | Mass: 24143.867 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #32: Protein | Mass: 23051.416 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #33: Protein | Mass: 17770.512 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #34: Protein | Mass: 11613.146 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #35: Protein | Mass: 14854.315 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #36: Protein | Mass: 14642.725 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #37: Protein | Mass: 11598.503 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #38: Protein | Mass: 13907.978 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #39: Protein | Mass: 15320.870 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #40: Protein | Mass: 13747.919 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #41: Protein | Mass: 7317.769 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #42: Protein | Mass: 10634.330 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #43: Protein | Mass: 10253.886 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #44: Protein | Mass: 10196.888 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #45: Protein | Mass: 9332.018 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #46: Protein | Mass: 10639.309 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #47: Protein | Mass: 9039.472 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #51: Protein | Mass: 17826.555 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 5 types, 392 molecules 






| #52: Chemical | ChemComp-ZN / #53: Chemical | ChemComp-MG / #54: Chemical | ChemComp-FME / | #55: Chemical | #56: Chemical | ChemComp-A1I09 / | Mass: 575.114 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C26H39ClN2O8S / Feature type: SUBJECT OF INVESTIGATION |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | N |
-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
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| Molecular weight |
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| Source (natural) |
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| Buffer solution | pH: 7.5 Details: 20 mM Tris-HCl, pH 7.5, 10 mM MgCl2, 50 mM NH4Cl, 0.1 mM EDTA, pH 8, 6 mM beta-mercaptoethanol | ||||||||||||||||||||||||
| 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 R2/2 | ||||||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K / Details: Blotting time 2.5 s Blot force 5 Waiting time 30 s |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TALOS ARCTICA |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1800 nm / Nominal defocus min: 400 nm |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 50 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of real images: 4008 |
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Processing
| EM software |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 389149 | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.98 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 61266 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Atomic model building | Protocol: RIGID BODY FIT / Space: REAL | ||||||||||||||||||||||||||||||||||||||||||||||||||||
| Atomic model building | PDB-ID: 7NHM Accession code: 7NHM / Source name: PDB / Type: experimental model |
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