+
Open data
-
Basic information
| Entry | Database: PDB / ID: 9tkp | |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Title | 70S Initiation Complex with extended IF2 bound (70S IC-I) | |||||||||
Components |
| |||||||||
Keywords | RIBOSOME / Translation Initiation / time-resolved cryo-electron microscopy / GTP hydrolysis / initiation factor 1 / initiation factor 2 | |||||||||
| Function / homology | Function and homology informationguanosine tetraphosphate binding / stringent response / ribosomal small subunit binding / transcription antitermination factor activity, RNA binding / ornithine decarboxylase inhibitor activity / misfolded RNA binding / Group I intron splicing / RNA folding / translational termination / transcriptional attenuation ...guanosine tetraphosphate binding / stringent response / ribosomal small subunit binding / transcription antitermination factor activity, RNA binding / ornithine decarboxylase inhibitor activity / misfolded RNA binding / Group I intron splicing / RNA folding / translational termination / transcriptional attenuation / endoribonuclease inhibitor activity / positive regulation of ribosome biogenesis / RNA-binding transcription regulator activity / four-way junction DNA binding / negative regulation of cytoplasmic translation / response to cold / regulation of mRNA stability / translation repressor activity / translation initiation factor activity / negative regulation of translational initiation / negative regulation of DNA-templated DNA replication initiation / mRNA regulatory element binding translation repressor activity / positive regulation of RNA splicing / response to reactive oxygen species / cytosolic ribosome assembly / regulation of DNA-templated transcription elongation / ribosome assembly / assembly of large subunit precursor of preribosome / transcription antitermination / regulation of cell growth / DNA endonuclease activity / molecular condensate scaffold activity / translational initiation / regulation of translation / DNA-templated transcription termination / response to radiation / maintenance of translational fidelity / mRNA 5'-UTR binding / transferase activity / large ribosomal subunit / ribosomal small subunit assembly / ribosome biogenesis / ribosome binding / protein folding / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / tRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / rRNA binding / negative regulation of translation / hydrolase activity / ribosome / translation / structural constituent of ribosome / response to antibiotic / negative regulation of DNA-templated transcription / mRNA binding / GTPase activity / GTP binding / DNA-templated transcription / DNA binding / RNA binding / zinc ion binding / membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å | |||||||||
Authors | Guerra, G.S. / Demo, G. | |||||||||
| Funding support | Czech Republic, 1items
| |||||||||
Citation | Journal: To Be PublishedTitle: Time-resolved visualization of IF1- and IF2-driven translation initiation in bacteria Authors: Guerra, G.S. / Zafar, H. / Ge, X. / Basu, R.S. / Huang, C. / Hassan, A.H. / Valdez, N.A. / Brabencova, S. / Slamova, L. / Mandava, C.S. / Gamper, H. / Hou, Y. / Gagnon, M.G. / Sanyal, S. / Demo, G. | |||||||||
| History |
|
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 9tkp.cif.gz | 3.7 MB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb9tkp.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9tkp.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tk/9tkp ftp://data.pdbj.org/pub/pdb/validation_reports/tk/9tkp | HTTPS FTP |
|---|
-Related structure data
| Related structure data | ![]() 56036MC ![]() 9tknC ![]() 9tkoC ![]() 9tkqC ![]() 9tkrC ![]() 9zn2C M: map data used to model this data C: citing same article ( |
|---|---|
| Similar structure data | Similarity search - Function & homology F&H Search |
-
Links
-
Assembly
| Deposited unit | ![]()
|
|---|---|
| 1 |
|
-
Components
-Small ribosomal subunit protein ... , 20 types, 20 molecules AAABACADAEAFAGAHAIAJAKALAMANAOAPAQARATAU
| #1: Protein | Mass: 26781.670 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
|---|---|
| #2: Protein | Mass: 26031.316 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #3: Protein | Mass: 23514.199 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #4: Protein | Mass: 17629.398 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #5: Protein | Mass: 15727.512 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #6: Protein | Mass: 20055.156 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #7: Protein | Mass: 14146.557 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #8: Protein | Mass: 14886.270 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein | Mass: 11755.597 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 13870.975 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #11: Protein | Mass: 13768.157 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #12: Protein | Mass: 13128.467 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #13: Protein | Mass: 11606.560 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #14: Protein | Mass: 10290.816 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #15: Protein | Mass: 9207.572 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #16: Protein | Mass: 9724.491 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #17: Protein | Mass: 9005.472 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #18: Protein | Mass: 10455.355 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #19: Protein | Mass: 9708.464 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #20: Protein | Mass: 8524.039 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+Large ribosomal subunit protein ... , 27 types, 27 molecules B0B1B2B3B5B6B7B8B9BABBBDBEBFBIBMBNBOBQBRBSBTBUBVBWBXBY
-50S ribosomal protein ... , 3 types, 3 molecules BCBKBP
| #32: Protein | Mass: 22277.535 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
|---|---|
| #37: Protein | Mass: 14894.362 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #41: Protein | Mass: 15312.269 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-RNA chain , 5 types, 5 molecules D1D2D3D4D5
| #51: RNA chain | Mass: 499031.562 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
|---|---|
| #52: RNA chain | Mass: 941305.250 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #53: RNA chain | Mass: 38813.133 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #54: RNA chain | Mass: 18057.820 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
| #55: RNA chain | Mass: 24802.785 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 1 types, 1 molecules F2
| #56: Protein | Mass: 98327.062 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
|---|
-Non-polymers , 3 types, 3 molecules 




| #57: Chemical | ChemComp-FME / |
|---|---|
| #58: Chemical | ChemComp-MG / |
| #59: Chemical | ChemComp-GTP / |
-Details
| Has ligand of interest | Y |
|---|---|
| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
|---|---|
| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
| Component | Name: 70S Initiation Complex with extended IF2 bound (70S IC-I) Type: RIBOSOME / Entity ID: #1-#56 / Source: NATURAL | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Molecular weight | Value: 2.5 MDa / Experimental value: NO | |||||||||||||||||||||||||
| Source (natural) | Organism: ![]() | |||||||||||||||||||||||||
| Buffer solution | pH: 7.5 | |||||||||||||||||||||||||
| Buffer component |
| |||||||||||||||||||||||||
| 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 R2/1 | |||||||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 95 % / Chamber temperature: 278 K |
-
Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
|---|---|
| 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: 2100 nm / Nominal defocus min: 500 nm / Alignment procedure: COMA FREE |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Average exposure time: 2 sec. / Electron dose: 40 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 17477 / Details: Movie-mode at 20 frames per second |
-
Processing
| EM software |
| ||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 1889196 | ||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 12354 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||
| Atomic model building | Protocol: OTHER / Space: REAL | ||||||||||||||||||||||||||||||||
| Atomic model building | PDB-ID: 6WDD Accession code: 6WDD / Source name: PDB / Type: experimental model | ||||||||||||||||||||||||||||||||
| Refinement | Highest resolution: 3 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) |
Movie
Controller
About Yorodumi






Czech Republic, 1items
Citation










PDBj
































FIELD EMISSION GUN
