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Yorodumi- EMDB-66122: Structure of E.coli ribosome in complex with an engineered arrest... -
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Open data
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Basic information
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| Title | Structure of E.coli ribosome in complex with an engineered arrest peptide and trigger factor | |||||||||
Map data | Map | |||||||||
Sample |
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Keywords | Ribosomal nascent chain / ribosomal arrest peptide / ribosomal translation / ribosome stalling / 70S Ribosome / RIBOSOME | |||||||||
| Function / homology | Function and homology information'de novo' cotranslational protein folding / stress response to copper ion / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / protein unfolding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity ...'de novo' cotranslational protein folding / stress response to copper ion / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / protein unfolding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / RNA-binding transcription regulator activity / positive regulation of ribosome biogenesis / negative regulation of cytoplasmic translation / four-way junction DNA binding / : / DnaA-L2 complex / translation repressor activity / regulation of mRNA stability / negative regulation of translational initiation / negative regulation of DNA-templated DNA replication initiation / protein folding chaperone / mRNA regulatory element binding translation repressor activity / assembly of large subunit precursor of preribosome / positive regulation of RNA splicing / ribosome assembly / regulation of DNA-templated transcription elongation / transcription elongation factor complex / cytosolic ribosome assembly / response to reactive oxygen species / DNA endonuclease activity / transcription antitermination / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / regulation of cell growth / DNA-templated transcription termination / response to radiation / maintenance of translational fidelity / mRNA 5'-UTR binding / protein transport / ribosome biogenesis / large ribosomal subunit / regulation of translation / ribosome binding / transferase activity / response to heat / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / 5S rRNA binding / ribosomal large subunit assembly / 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 / cell division / response to antibiotic / negative regulation of DNA-templated transcription / mRNA binding / DNA binding / RNA binding / zinc ion binding / identical protein binding / membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.76 Å | |||||||||
Authors | Sriramoju MK / Ko TP / Draczkowski P / Hsu STD | |||||||||
| Funding support | Taiwan, 2 items
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Citation | Journal: Nucleic Acids Res. / Year: 2025Title: Structural basis of enhanced stalling efficiency of an engineered ribosome arrest peptide Authors: Sriramoju MK / Ko TP / Draczkowski P / Hsu STD | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_66122.map.gz | 456.8 MB | EMDB map data format | |
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| Header (meta data) | emd-66122-v30.xml emd-66122.xml | 83.9 KB 83.9 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_66122_fsc.xml | 20.4 KB | Display | FSC data file |
| Images | emd_66122.png | 144.3 KB | ||
| Filedesc metadata | emd-66122.cif.gz | 15.2 KB | ||
| Others | emd_66122_half_map_1.map.gz emd_66122_half_map_2.map.gz | 843.2 MB 843.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-66122 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-66122 | HTTPS FTP |
-Validation report
| Summary document | emd_66122_validation.pdf.gz | 993.1 KB | Display | EMDB validaton report |
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| Full document | emd_66122_full_validation.pdf.gz | 992.7 KB | Display | |
| Data in XML | emd_66122_validation.xml.gz | 30.4 KB | Display | |
| Data in CIF | emd_66122_validation.cif.gz | 40.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-66122 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-66122 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9wnrMC ![]() 9wnqC 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_66122.map.gz / Format: CCP4 / Size: 909.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.1 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: HalfMap-B
| File | emd_66122_half_map_1.map | ||||||||||||
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| Annotation | HalfMap-B | ||||||||||||
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| Density Histograms |
-Half map: HalfMap-A
| File | emd_66122_half_map_2.map | ||||||||||||
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| Annotation | HalfMap-A | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
+Entire : E.coli 70S Ribosome in complex with eRAP
+Supramolecule #1: E.coli 70S Ribosome in complex with eRAP
+Macromolecule #1: Large ribosomal subunit protein bL28
+Macromolecule #2: Large ribosomal subunit protein uL29
+Macromolecule #3: Large ribosomal subunit protein uL30
+Macromolecule #4: Large ribosomal subunit protein bL32
+Macromolecule #5: Large ribosomal subunit protein bL33
+Macromolecule #6: 50S ribosomal protein L34
+Macromolecule #7: Large ribosomal subunit protein bL35
+Macromolecule #8: 50S ribosomal protein L36
+Macromolecule #10: 30S ribosomal protein S2
+Macromolecule #11: 30S ribosomal protein S3
+Macromolecule #12: 30S ribosomal protein S4
+Macromolecule #13: 30S ribosomal protein S5
+Macromolecule #14: 30S ribosomal protein S6, fully modified isoform
+Macromolecule #15: 30S ribosomal protein S7
+Macromolecule #16: 30S ribosomal protein S8
+Macromolecule #17: 30S ribosomal protein S9
+Macromolecule #18: 30S ribosomal protein S10
+Macromolecule #19: Small ribosomal subunit protein uS11
+Macromolecule #20: Small ribosomal subunit protein uS12
+Macromolecule #21: 30S ribosomal protein S13
+Macromolecule #22: 30S ribosomal protein S14
+Macromolecule #23: 30S ribosomal protein S15
+Macromolecule #24: 30S ribosomal protein S16
+Macromolecule #25: 30S ribosomal protein S17
+Macromolecule #26: 30S ribosomal protein S18
+Macromolecule #27: 30S ribosomal protein S19
+Macromolecule #28: 30S ribosomal protein S20
+Macromolecule #29: 30S ribosomal protein S21
+Macromolecule #30: Trigger factor
+Macromolecule #35: Large ribosomal subunit protein uL2
+Macromolecule #36: 50S ribosomal protein L3
+Macromolecule #37: 50S ribosomal protein L4
+Macromolecule #38: Large ribosomal subunit protein uL5
+Macromolecule #39: Large ribosomal subunit protein uL6
+Macromolecule #40: 50S ribosomal protein L9
+Macromolecule #41: 50S ribosomal protein L13
+Macromolecule #42: 50S ribosomal protein L14
+Macromolecule #43: 50S ribosomal protein L15
+Macromolecule #44: 50S ribosomal protein L16
+Macromolecule #45: Large ribosomal subunit protein bL17
+Macromolecule #46: Large ribosomal subunit protein uL18
+Macromolecule #47: Large ribosomal subunit protein bL19
+Macromolecule #48: Large ribosomal subunit protein bL20
+Macromolecule #49: 50S ribosomal protein L21
+Macromolecule #50: 50S ribosomal protein L22
+Macromolecule #51: Large ribosomal subunit protein uL23
+Macromolecule #52: 50S ribosomal protein L24
+Macromolecule #53: 50S ribosomal protein L25
+Macromolecule #55: Large ribosomal subunit protein bL27
+Macromolecule #56: eRAP-NC
+Macromolecule #9: 16S rRNA
+Macromolecule #31: E-tRNA
+Macromolecule #32: P-tRNA(PRO), A-tRNA(PRO)
+Macromolecule #33: 5S rRNA
+Macromolecule #34: 23S rRNA
+Macromolecule #54: mRNA
+Macromolecule #57: ZINC ION
+Macromolecule #58: PROLINE
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 0.42 mg/mL |
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| Buffer | pH: 7.6 Details: 20 mM HEPES (pH 7.6), 140 mM NH4Cl, 25 mM MgCl2, 2 mM DTT |
| Grid | Model: Quantifoil / Support film - Material: CARBON / Support film - topology: CONTINUOUS |
| Vitrification | Cryogen name: NITROGEN / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number real images: 15280 / Average exposure time: 2.5 sec. / Average electron dose: 38.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.0 µm |
| Sample stage | Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Keywords
Authors
Taiwan, 2 items
Citation








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Processing
FIELD EMISSION GUN


