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Yorodumi- EMDB-12242: Bacterial 30S ribosomal subunit assembly complex state E (body domain) -
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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-12242 | |||||||||
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| Title | Bacterial 30S ribosomal subunit assembly complex state E (body domain) | |||||||||
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Sample |
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Keywords | Cryo-EM / 30S biogenesis / ribosome assembly / RbfA / RsgA / YjeQ / RimP / KsgA / RsmA / RIBOSOME | |||||||||
| Function / homology | Function and homology informationornithine decarboxylase inhibitor activity / ribosomal small subunit binding / misfolded RNA binding / Group I intron splicing / RNA folding / four-way junction DNA binding / regulation of mRNA stability / negative regulation of translational initiation / response to cold / mRNA regulatory element binding translation repressor activity ...ornithine decarboxylase inhibitor activity / ribosomal small subunit binding / misfolded RNA binding / Group I intron splicing / RNA folding / four-way junction DNA binding / regulation of mRNA stability / negative regulation of translational initiation / response to cold / mRNA regulatory element binding translation repressor activity / positive regulation of RNA splicing / DNA endonuclease activity / maturation of SSU-rRNA / transcription antitermination / DNA-templated transcription termination / maintenance of translational fidelity / mRNA 5'-UTR binding / ribosome biogenesis / regulation of translation / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytoplasmic translation / tRNA binding / rRNA binding / structural constituent of ribosome / ribosome / translation / response to antibiotic / DNA damage response / zinc ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.75 Å | |||||||||
Authors | Schedlbauer A / Iturrioz I | |||||||||
| Funding support | Spain, 2 items
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Citation | Journal: Sci Adv / Year: 2021Title: A conserved rRNA switch is central to decoding site maturation on the small ribosomal subunit. Authors: Andreas Schedlbauer / Idoia Iturrioz / Borja Ochoa-Lizarralde / Tammo Diercks / Jorge Pedro López-Alonso / José Luis Lavin / Tatsuya Kaminishi / Retina Çapuni / Neha Dhimole / Elisa de ...Authors: Andreas Schedlbauer / Idoia Iturrioz / Borja Ochoa-Lizarralde / Tammo Diercks / Jorge Pedro López-Alonso / José Luis Lavin / Tatsuya Kaminishi / Retina Çapuni / Neha Dhimole / Elisa de Astigarraga / David Gil-Carton / Paola Fucini / Sean R Connell / ![]() Abstract: While a structural description of the molecular mechanisms guiding ribosome assembly in eukaryotic systems is emerging, bacteria use an unrelated core set of assembly factors for which high- ...While a structural description of the molecular mechanisms guiding ribosome assembly in eukaryotic systems is emerging, bacteria use an unrelated core set of assembly factors for which high-resolution structural information is still missing. To address this, we used single-particle cryo-electron microscopy to visualize the effects of bacterial ribosome assembly factors RimP, RbfA, RsmA, and RsgA on the conformational landscape of the 30 ribosomal subunit and obtained eight snapshots representing late steps in the folding of the decoding center. Analysis of these structures identifies a conserved secondary structure switch in the 16 ribosomal RNA central to decoding site maturation and suggests both a sequential order of action and molecular mechanisms for the assembly factors in coordinating and controlling this switch. Structural and mechanistic parallels between bacterial and eukaryotic systems indicate common folding features inherent to all ribosomes. | |||||||||
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Structure visualization
| Movie |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_12242.map.gz | 182.7 MB | EMDB map data format | |
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| Header (meta data) | emd-12242-v30.xml emd-12242.xml | 32.6 KB 32.6 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_12242_fsc.xml | 14.1 KB | Display | FSC data file |
| Images | emd_12242.png | 169.2 KB | ||
| Masks | emd_12242_msk_1.map | 244.1 MB | Mask map | |
| Filedesc metadata | emd-12242.cif.gz | 8.6 KB | ||
| Others | emd_12242_half_map_1.map.gz emd_12242_half_map_2.map.gz | 183.1 MB 183.1 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-12242 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-12242 | HTTPS FTP |
-Validation report
| Summary document | emd_12242_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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| Full document | emd_12242_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | emd_12242_validation.xml.gz | 21 KB | Display | |
| Data in CIF | emd_12242_validation.cif.gz | 27.6 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-12242 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-12242 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7bogMC ![]() 7af3C ![]() 7af5C ![]() 7af8C ![]() 7afaC ![]() 7afdC ![]() 7afhC ![]() 7afiC ![]() 7afkC ![]() 7aflC ![]() 7afnC ![]() 7afoC ![]() 7afqC ![]() 7afrC ![]() 7bodC ![]() 7boeC ![]() 7bofC ![]() 7bohC ![]() 7boiC ![]() 7narC ![]() 7nasC ![]() 7natC ![]() 7nauC ![]() 7navC ![]() 7naxC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data |
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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_12242.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.05 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Mask #1
| File | emd_12242_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: #2
| File | emd_12242_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_12242_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
+Entire : Bacterial 30S ribosomal subunit assembly complex state E (body domain)
+Supramolecule #1: Bacterial 30S ribosomal subunit assembly complex state E (body domain)
+Supramolecule #2: Bacterial 30S ribosomal subunit assembly
+Supramolecule #3: 30S ribosome-binding factor
+Macromolecule #1: 16S rRNA
+Macromolecule #2: 30S ribosomal protein S4
+Macromolecule #3: 30S ribosomal protein S5
+Macromolecule #4: 30S ribosomal protein S6
+Macromolecule #5: 30S ribosomal protein S8
+Macromolecule #6: 30S ribosomal protein S11
+Macromolecule #7: 30S ribosomal protein S12
+Macromolecule #8: 30S ribosomal protein S15
+Macromolecule #9: 30S ribosomal protein S16
+Macromolecule #10: 30S ribosomal protein S17
+Macromolecule #11: 30S ribosomal protein S18
+Macromolecule #12: 30S ribosomal protein S20
+Macromolecule #13: 30S ribosome-binding factor
+Macromolecule #14: MAGNESIUM ION
-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: 7.8 |
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| Grid | Model: Quantifoil R2/2 / Support film - Material: CARBON / Support film - topology: CONTINUOUS |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK III |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Average electron dose: 38.8 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi


Keywords
Authors
Spain, 2 items
Citation
UCSF Chimera

























































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