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Open data
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Basic information
| Entry | ![]() | |||||||||||||||||||||
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| Title | 30S mRNA delivery complex (consensus) | |||||||||||||||||||||
Map data | 30S-RNAP delivery consensus | |||||||||||||||||||||
Sample |
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Keywords | Transcription / translation / coupling / Ribosome. / RIBOSOME | |||||||||||||||||||||
| Function / homology | Function and homology informationpositive regulation of cytoplasmic translation / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / negative regulation of cytoplasmic translation / four-way junction DNA binding / regulation of mRNA stability / positive regulation of RNA splicing ...positive regulation of cytoplasmic translation / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / negative regulation of cytoplasmic translation / four-way junction DNA binding / regulation of mRNA stability / positive regulation of RNA splicing / regulation of DNA-templated transcription elongation / transcription elongation factor complex / DNA endonuclease activity / transcription antitermination / 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 / single-stranded RNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / response to antibiotic / mRNA binding / RNA binding / zinc ion binding / membrane / cytoplasm / cytosol Similarity search - Function | |||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.5 Å | |||||||||||||||||||||
Authors | Rahil H / Weixlbaumer A / Webster MW | |||||||||||||||||||||
| Funding support | European Union, France, United States, United Kingdom, 6 items
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Citation | Journal: Science / Year: 2024Title: Molecular basis of mRNA delivery to the bacterial ribosome. Authors: Michael W Webster / Adrien Chauvier / Huma Rahil / Andrea Graziadei / Kristine Charles / Nataliya Miropolskaya / Maria Takacs / Charlotte Saint-André / Juri Rappsilber / Nils G Walter / Albert Weixlbaumer / ![]() Abstract: Protein synthesis begins with the formation of a ribosome-messenger RNA (mRNA) complex. In bacteria, the small ribosomal subunit (30) is recruited to many mRNAs through base pairing with the Shine- ...Protein synthesis begins with the formation of a ribosome-messenger RNA (mRNA) complex. In bacteria, the small ribosomal subunit (30) is recruited to many mRNAs through base pairing with the Shine-Dalgarno (SD) sequence and RNA binding by ribosomal protein bS1. Translation can initiate on nascent mRNAs, and RNA polymerase (RNAP) can promote the recruitment of the pioneering 30. Here, we examined 30 recruitment to nascent mRNAs using cryo-electron microscopy, single-molecule fluorescence colocalization, and in-cell cross-linking mass spectrometry. We show that bS1 delivers the mRNA to the ribosome for SD duplex formation and 30 activation. Additionally, bS1 and RNAP stimulate translation initiation. Our work provides a mechanistic framework for how the SD duplex, ribosomal proteins, and RNAP cooperate in 30 recruitment to mRNAs and establish transcription-translation coupling. | |||||||||||||||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_51620.map.gz | 776.8 MB | EMDB map data format | |
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| Header (meta data) | emd-51620-v30.xml emd-51620.xml | 41.8 KB 41.8 KB | Display Display | EMDB header |
| Images | emd_51620.png | 46.2 KB | ||
| Filedesc metadata | emd-51620.cif.gz | 11.9 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-51620 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-51620 | HTTPS FTP |
-Validation report
| Summary document | emd_51620_validation.pdf.gz | 541.6 KB | Display | EMDB validaton report |
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| Full document | emd_51620_full_validation.pdf.gz | 541.1 KB | Display | |
| Data in XML | emd_51620_validation.xml.gz | 8.3 KB | Display | |
| Data in CIF | emd_51620_validation.cif.gz | 9.7 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51620 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-51620 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9guuMC ![]() 9gr1C ![]() 9gupC ![]() 9guqC ![]() 9gurC ![]() 9gusC ![]() 9gutC ![]() 9guvC ![]() 9guwC ![]() 9guxC C: citing same article ( M: atomic model generated by this map |
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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_51620.map.gz / Format: CCP4 / Size: 824 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | 30S-RNAP delivery consensus | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.84 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
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Sample components
+Entire : 30S ribosomal subunit
+Supramolecule #1: 30S ribosomal subunit
+Macromolecule #1: 16S ribosomal RNA
+Macromolecule #23: tRNA(fmet) P-site
+Macromolecule #24: mRNA
+Macromolecule #2: 30S ribosomal protein S1
+Macromolecule #3: 30S ribosomal protein S2
+Macromolecule #4: Small ribosomal subunit protein uS3
+Macromolecule #5: Small ribosomal subunit protein uS4
+Macromolecule #6: 30S ribosomal protein S5
+Macromolecule #7: Small ribosomal subunit protein bS6
+Macromolecule #8: 30S ribosomal protein S7
+Macromolecule #9: 30S ribosomal protein S8
+Macromolecule #10: 30S ribosomal protein S9
+Macromolecule #11: 30S ribosomal protein S10
+Macromolecule #12: 30S ribosomal protein S11
+Macromolecule #13: 30S ribosomal protein S12
+Macromolecule #14: 30S ribosomal protein S13
+Macromolecule #15: 30S ribosomal protein S14
+Macromolecule #16: Small ribosomal subunit protein uS15
+Macromolecule #17: 30S ribosomal protein S16
+Macromolecule #18: 30S ribosomal protein S17
+Macromolecule #19: 30S ribosomal protein S18
+Macromolecule #20: 30S ribosomal protein S19
+Macromolecule #21: 30S ribosomal protein S20
+Macromolecule #22: 30S ribosomal protein S21
+Macromolecule #25: 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: 7.4 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 49.95 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
France,
United States,
United Kingdom, 6 items
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Y (Row.)
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Processing
FIELD EMISSION GUN

