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Open data
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Basic information
| Entry | Database: PDB / ID: 9t6m | ||||||||||||||||||||||||||||||
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| Title | E. coli 70S ribosome from delta-10 strain | ||||||||||||||||||||||||||||||
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Keywords | RIBOSOME / RNA modifications / ribosome biogenesis / maturation | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationnegative regulation of cytoplasmic translational initiation / transcription antitermination factor activity, RNA binding / ornithine decarboxylase inhibitor activity / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / positive regulation of ribosome biogenesis / RNA-binding transcription regulator activity ...negative regulation of cytoplasmic translational initiation / transcription antitermination factor activity, RNA binding / ornithine decarboxylase inhibitor activity / misfolded RNA binding / Group I intron splicing / RNA folding / 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 / regulation of mRNA stability / translation repressor 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 / regulation of DNA-templated transcription elongation / response to reactive oxygen species / cytosolic ribosome assembly / ribosome assembly / assembly of large subunit precursor of preribosome / transcription antitermination / DNA endonuclease activity / regulation of cell growth / translational initiation / DNA-templated transcription termination / response to radiation / maintenance of translational fidelity / mRNA 5'-UTR binding / regulation of translation / large ribosomal subunit / transferase activity / ribosomal small subunit assembly / ribosome binding / ribosomal small subunit biogenesis / ribosome biogenesis / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / ribosome / translation / structural constituent of ribosome / response to antibiotic / negative regulation of DNA-templated transcription / hydrolase activity / mRNA binding / DNA binding / DNA-templated transcription / RNA binding / zinc ion binding / membrane / cytosol / cytoplasm Similarity search - Function | ||||||||||||||||||||||||||||||
| Biological species | ![]() | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 1.87 Å | ||||||||||||||||||||||||||||||
Authors | Larsson, D.S.D. / Selmer, M. | ||||||||||||||||||||||||||||||
| Funding support | Sweden, 3items
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Citation | Journal: Nucleic Acids Res / Year: 2026Title: 23S rRNA modifications stimulate catalytic activity and prevent the formation of alternative structures. Authors: Daniel S D Larsson / Aivar Liiv / Rya Ero / Jaanus Remme / Maria Selmer / ![]() Abstract: Ribosomal RNA (rRNA) modifications cluster around the peptidyl transferase centre (PTC), the catalytic centre of the ribosome, yet their collective functional roles remain unclear. Here we analyse ...Ribosomal RNA (rRNA) modifications cluster around the peptidyl transferase centre (PTC), the catalytic centre of the ribosome, yet their collective functional roles remain unclear. Here we analyse Escherichia coli ribosomes lacking 11 or 12 modifications near the PTC. Using kinetic assays, we show these hypo-modified ribosomes catalyse peptide bond formation at rates twofold to threefold lower than wild-type and exhibit reduced thermal stability. Cryo-electron microscopy of hypo-modified ribosomes reveals multiple alternative conformations of the PTC and exit tunnel regions, disrupting native stacking and hydrogen bonding critical for positioning of transfer RNA substrates. These findings indicate that rRNA modifications stabilize the native PTC structure, preventing formation of alternative, nonfunctional conformations and thereby enhancing catalytic efficiency. Our study provides insight into how rRNA modifications fine-tune ribosome function by maintaining structural integrity essential for efficient translation. #1: Journal: Biorxiv / Year: 2026Title: Ribosomal RNA modifications around the peptidyl transfer center stimulate catalytic activity and prevent the formation of alternative structures Authors: Larsson, D.S.D. / Liiv, A. / Ero, R. / Remme, J. / Selmer, M. | ||||||||||||||||||||||||||||||
| 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 | 9t6m.cif.gz | 4.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9t6m.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9t6m.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t6/9t6m ftp://data.pdbj.org/pub/pdb/validation_reports/t6/9t6m | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 55618MC ![]() 9syhC ![]() 9t0yC ![]() 9t19C ![]() 9t1aC ![]() 9t1bC ![]() 9t1cC ![]() 9t1eC ![]() 9t1fC ![]() 9t1gC ![]() 9t1hC ![]() 9t1iC ![]() 9t1jC ![]() 9t2jC ![]() 9t2kC ![]() 9t2lC ![]() 9t2mC ![]() 9t2nC ![]() 9t2oC ![]() 9t2pC ![]() 9t2qC ![]() 9t2rC ![]() 9t2sC ![]() 9t8kC ![]() 9t8lC ![]() 9t8mC ![]() 9t8nC ![]() 9t8oC ![]() 9t8pC ![]() 9t8qC ![]() 9t8tC 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
-RNA chain , 6 types, 7 molecules AXYZ5ab
| #1: RNA chain | Mass: 499873.406 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() | ||||
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| #22: RNA chain | Mass: 39004.727 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() | ||||
| #23: RNA chain | Mass: 24750.010 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() | ||||
| #24: RNA chain | Mass: 24848.918 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #25: RNA chain | | Mass: 941726.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #26: RNA chain | | Mass: 38790.090 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Small ribosomal subunit protein ... , 20 types, 20 molecules BCDEFGHIJKLMNOPQRSTU
| #2: Protein | Mass: 26781.670 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #3: Protein | Mass: 26031.316 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #4: Protein | Mass: 23514.199 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #5: Protein | Mass: 17629.398 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #6: Protein | Mass: 15727.512 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #7: Protein | Mass: 20055.156 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #8: Protein | Mass: 14146.557 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein | Mass: 14886.270 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 11755.597 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #11: Protein | Mass: 13871.959 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #12: Protein | Mass: 13814.249 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #13: Protein | Mass: 13128.467 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #14: Protein | Mass: 11606.560 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #15: Protein | Mass: 10290.816 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #16: Protein | Mass: 9207.572 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #17: Protein | Mass: 9724.491 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #18: Protein | Mass: 9005.472 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #19: Protein | Mass: 10455.355 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #20: Protein | Mass: 9708.464 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #21: Protein | Mass: 8524.039 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+Large ribosomal subunit protein ... , 29 types, 29 molecules cdefghijklmnopqrstuvwxyz01234
-Non-polymers , 6 types, 5201 molecules 










| #56: Chemical | ChemComp-K / #57: Chemical | ChemComp-MG / #58: Chemical | ChemComp-SR0 / #59: Chemical | ChemComp-PUT / #60: Chemical | #61: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | Y |
-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: 70S ribosome / Type: RIBOSOME / Entity ID: #1-#55 / Source: NATURAL | |||||||||||||||||||||||||||||||||||||||||||||
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| Molecular weight | Value: 2.5 MDa / Experimental value: NO | |||||||||||||||||||||||||||||||||||||||||||||
| Source (natural) | Organism: ![]() | |||||||||||||||||||||||||||||||||||||||||||||
| Buffer solution | pH: 7.5 / Details: HEPES-polymix buffer (pH-7.5) | |||||||||||||||||||||||||||||||||||||||||||||
| Buffer component |
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| 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 / 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: 1400 nm / Nominal defocus min: 600 nm / Cs: 2.7 mm / C2 aperture diameter: 50 µm |
| Image recording | Electron dose: 30 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 8488 |
| EM imaging optics | Energyfilter name: GIF Bioquantum / Energyfilter slit width: 20 eV |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 863376 | ||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 1.87 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 582240 / Algorithm: FOURIER SPACE / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||
| Atomic model building | B value: 87.77 / Protocol: FLEXIBLE FIT / Space: REAL | ||||||||||||||||||||||||||||||||||||||||
| Atomic model building | PDB-ID: 9T0Y Accession code: 9T0Y / Source name: PDB / Type: experimental model | ||||||||||||||||||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi






Sweden, 3items
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FIELD EMISSION GUN