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Open data
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Basic information
| Entry | ![]() | ||||||||||||
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| Title | E. coli 70S ribosome from delta-9 strain | ||||||||||||
Map data | Main map, unsharpened | ||||||||||||
Sample |
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Keywords | RNA modifications / ribosome biogenesis / maturation / RIBOSOME | ||||||||||||
| 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 / regulation of translation / mRNA 5'-UTR binding / large ribosomal subunit / transferase activity / ribosomal small subunit assembly / ribosome binding / ribosome biogenesis / ribosomal small subunit biogenesis / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / tRNA binding / cytoplasmic translation / 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 | single particle reconstruction / cryo EM / Resolution: 1.87 Å | ||||||||||||
Authors | Larsson DSD / Selmer M | ||||||||||||
| Funding support | Sweden, 3 items
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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 DSD / Liiv A / Ero R / Remme J / Selmer M | ||||||||||||
| History |
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_55415.map.gz | 409.8 MB | EMDB map data format | |
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| Header (meta data) | emd-55415-v30.xml emd-55415.xml | 87.7 KB 87.7 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_55415_fsc.xml | 17.9 KB | Display | FSC data file |
| Images | emd_55415.png | 93.4 KB | ||
| Filedesc metadata | emd-55415.cif.gz | 16.1 KB | ||
| Others | emd_55415_additional_1.map.gz emd_55415_additional_2.map.gz emd_55415_half_map_1.map.gz emd_55415_half_map_2.map.gz | 295.3 MB 1.1 MB 412.6 MB 412.8 MB | ||
| Archive directory | https://data.pdbj.org/pub/emdb/structures/EMD-55415 ftp://data.pdbj.org/pub/emdb/structures/EMD-55415 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9t0yMC ![]() 9syhC ![]() 9t19C ![]() 9t1aC ![]() 9t1bC ![]() 9t1cC ![]() 9t1eC ![]() 9t1fC ![]() 9t1gC ![]() 9t1hC ![]() 9t1iC ![]() 9t1jC ![]() 9t2jC ![]() 9t2kC ![]() 9t2lC ![]() 9t2mC ![]() 9t2nC ![]() 9t2oC ![]() 9t2pC ![]() 9t2qC ![]() 9t2rC ![]() 9t2sC ![]() 9t6mC ![]() 9t8kC ![]() 9t8lC ![]() 9t8mC ![]() 9t8nC ![]() 9t8oC ![]() 9t8pC ![]() 9t8qC ![]() 9t8rC ![]() 9t8sC ![]() 9t8tC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_55415.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Main map, unsharpened | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.8215 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: B-factor sharpened map, low-pass filtered to local resolution
| File | emd_55415_additional_1.map | ||||||||||||
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| Annotation | B-factor sharpened map, low-pass filtered to local resolution | ||||||||||||
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| Density Histograms |
-Additional map: Mask for focused classification of the PTC region
| File | emd_55415_additional_2.map | ||||||||||||
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| Annotation | Mask for focused classification of the PTC region | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_55415_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_55415_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
+Entire : 70S ribosome
+Supramolecule #1: 70S ribosome
+Macromolecule #1: 16S rRNA
+Macromolecule #22: mRNA
+Macromolecule #23: tRNA(Phe)
+Macromolecule #24: tRNA(fMet)
+Macromolecule #25: 23S rRNA
+Macromolecule #26: 5S rRNA
+Macromolecule #2: Small ribosomal subunit protein uS2
+Macromolecule #3: Small ribosomal subunit protein uS3
+Macromolecule #4: Small ribosomal subunit protein uS4
+Macromolecule #5: Small ribosomal subunit protein uS5
+Macromolecule #6: Small ribosomal subunit protein bS6, fully modified isoform
+Macromolecule #7: Small ribosomal subunit protein uS7
+Macromolecule #8: Small ribosomal subunit protein uS8
+Macromolecule #9: Small ribosomal subunit protein uS9
+Macromolecule #10: Small ribosomal subunit protein uS10
+Macromolecule #11: Small ribosomal subunit protein uS11
+Macromolecule #12: Small ribosomal subunit protein uS12
+Macromolecule #13: Small ribosomal subunit protein uS13
+Macromolecule #14: Small ribosomal subunit protein uS14
+Macromolecule #15: Small ribosomal subunit protein uS15
+Macromolecule #16: Small ribosomal subunit protein bS16
+Macromolecule #17: Small ribosomal subunit protein uS17
+Macromolecule #18: Small ribosomal subunit protein bS18
+Macromolecule #19: Small ribosomal subunit protein uS19
+Macromolecule #20: Small ribosomal subunit protein bS20
+Macromolecule #21: Small ribosomal subunit protein bS21
+Macromolecule #27: Large ribosomal subunit protein uL2
+Macromolecule #28: Large ribosomal subunit protein uL3
+Macromolecule #29: Large ribosomal subunit protein uL4
+Macromolecule #30: Large ribosomal subunit protein uL5
+Macromolecule #31: Large ribosomal subunit protein uL6
+Macromolecule #32: Large ribosomal subunit protein bL9
+Macromolecule #33: Large ribosomal subunit protein uL13
+Macromolecule #34: Large ribosomal subunit protein uL14
+Macromolecule #35: Large ribosomal subunit protein uL15
+Macromolecule #36: Large ribosomal subunit protein uL16
+Macromolecule #37: Large ribosomal subunit protein bL17
+Macromolecule #38: Large ribosomal subunit protein uL18
+Macromolecule #39: Large ribosomal subunit protein bL19
+Macromolecule #40: Large ribosomal subunit protein bL20
+Macromolecule #41: Large ribosomal subunit protein bL21
+Macromolecule #42: Large ribosomal subunit protein uL22
+Macromolecule #43: Large ribosomal subunit protein uL23
+Macromolecule #44: Large ribosomal subunit protein uL24
+Macromolecule #45: Large ribosomal subunit protein bL25
+Macromolecule #46: Large ribosomal subunit protein bL27
+Macromolecule #47: Large ribosomal subunit protein bL28
+Macromolecule #48: Large ribosomal subunit protein uL29
+Macromolecule #49: Large ribosomal subunit protein uL30
+Macromolecule #50: Large ribosomal subunit protein bL32
+Macromolecule #51: Large ribosomal subunit protein bL33
+Macromolecule #52: Large ribosomal subunit protein bL34
+Macromolecule #53: Large ribosomal subunit protein bL35
+Macromolecule #54: Large ribosomal subunit protein bL36A
+Macromolecule #55: Large ribosomal subunit protein bL31A
+Macromolecule #56: POTASSIUM ION
+Macromolecule #57: MAGNESIUM ION
+Macromolecule #58: N~1~-(3-azaniumylpropyl)butane-1,4-diaminium
+Macromolecule #59: 1,4-DIAMINOBUTANE
+Macromolecule #60: ZINC ION
+Macromolecule #61: water
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.5 Component:
Details: HEPES-polymix buffer (pH-7.5) | |||||||||||||||||||||||||||
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| Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 300 / Support film - #0 - Film type ID: 1 / Support film - #0 - Material: CARBON / Support film - #0 - topology: HOLEY / Support film - #1 - Film type ID: 2 / Support film - #1 - Material: CARBON / Support film - #1 - topology: CONTINUOUS / Support film - #1 - Film thickness: 2 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 20 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.04 kPa | |||||||||||||||||||||||||||
| Vitrification | Cryogen name: ETHANE / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Number real images: 9692 / Average electron dose: 30.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
Sweden, 3 items
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Y (Row.)
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Processing
FIELD EMISSION GUN

