+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-15116 | |||||||||
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Title | Structural insights into the binding of bS1 to the ribosome | |||||||||
Map data | Sharpened Map | |||||||||
Sample |
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Keywords | bS1 / Ribosome / Cryo-EM / Translation | |||||||||
Function / homology | Function and homology information RNA secondary structure unwinding / positive regulation of cytoplasmic translation / negative regulation of cytoplasmic translational initiation / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity ...RNA secondary structure unwinding / positive regulation of cytoplasmic translation / negative regulation of cytoplasmic translational initiation / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / 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 / DnaA-L2 complex / four-way junction DNA binding / translation repressor activity / negative regulation of translational initiation / negative regulation of DNA-templated DNA replication initiation / regulation of mRNA stability / mRNA regulatory element binding translation repressor activity / ribosome assembly / assembly of large subunit precursor of preribosome / positive regulation of RNA splicing / cytosolic ribosome assembly / transcription elongation factor complex / regulation of DNA-templated transcription elongation / DNA endonuclease activity / response to reactive oxygen species / transcription antitermination / regulation of cell growth / translational initiation / DNA-templated transcription termination / maintenance of translational fidelity / response to radiation / mRNA 5'-UTR binding / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / large ribosomal subunit / ribosome biogenesis / ribosome binding / regulation of translation / ribosomal small subunit assembly / large ribosomal subunit rRNA binding / 5S rRNA binding / transferase activity / small ribosomal subunit / cytosolic small ribosomal subunit / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit / tRNA binding / molecular adaptor activity / negative regulation of translation / single-stranded RNA binding / rRNA binding / ribosome / structural constituent of ribosome / translation / response to antibiotic / negative regulation of DNA-templated transcription / mRNA binding / DNA binding / RNA binding / zinc ion binding / membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Escherichia coli (E. coli) / Escherichia coli K-12 (bacteria) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.42 Å | |||||||||
Authors | D'Urso G / Chat S / Gillet R / Giudice E | |||||||||
Funding support | France, 1 items
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Citation | Journal: Nucleic Acids Res / Year: 2023 Title: Structural insights into the binding of bS1 to the ribosome. Authors: Gaetano D'Urso / Sophie Chat / Reynald Gillet / Emmanuel Giudice / Abstract: The multidomain ribosomal protein bS1 is the biggest and the most flexible and dynamic protein in the 30S small subunit. Despite being essential for mRNA recruitment and its primary role in the ...The multidomain ribosomal protein bS1 is the biggest and the most flexible and dynamic protein in the 30S small subunit. Despite being essential for mRNA recruitment and its primary role in the accommodation of the start codon within the decoding centre, there has not yet been a high-resolution description of its structure. Here, we present a 3D atomic model of OB1 and OB2, bS1's first two N-terminal domains, bound to an elongation-competent 70S ribosome. Our structure reveals that, as previously reported, bS1 is anchored both by a π-stacking to the 30S subunit and via a salt bridge with the Zn2+ pocket of bS1. These contacts are further stabilized by other interactions with additional residues on OB1. Our model also shows a new conformation of OB2, interacting with the Shine-Dalgarno portion of the mRNA. This study confirms that OB1 plays an anchoring role, but also highlights a novel function for OB2, which is directly involved in the modulation and support of mRNA binding and accommodation on the ribosome. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_15116.map.gz | 408.3 MB | EMDB map data format | |
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Header (meta data) | emd-15116-v30.xml emd-15116.xml | 78 KB 78 KB | Display Display | EMDB header |
Images | emd_15116.png | 69 KB | ||
Masks | emd_15116_msk_1.map | 512 MB | Mask map | |
Filedesc metadata | emd-15116.cif.gz | 15.2 KB | ||
Others | emd_15116_additional_1.map.gz emd_15116_half_map_1.map.gz emd_15116_half_map_2.map.gz | 412.6 MB 414.5 MB 414.7 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-15116 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-15116 | HTTPS FTP |
-Validation report
Summary document | emd_15116_validation.pdf.gz | 1 MB | Display | EMDB validaton report |
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Full document | emd_15116_full_validation.pdf.gz | 1 MB | Display | |
Data in XML | emd_15116_validation.xml.gz | 18.9 KB | Display | |
Data in CIF | emd_15116_validation.cif.gz | 22.6 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-15116 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-15116 | HTTPS FTP |
-Related structure data
Related structure data | 8a3lMC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_15116.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | Sharpened Map | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.893 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_15116_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: RELION Map
File | emd_15116_additional_1.map | ||||||||||||
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Annotation | RELION Map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: RELION -Half-Map
File | emd_15116_half_map_1.map | ||||||||||||
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Annotation | RELION -Half-Map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: RELION Half-Map
File | emd_15116_half_map_2.map | ||||||||||||
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Annotation | RELION Half-Map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
+Entire : Elongation competent ribosome in complex with bS1
+Supramolecule #1: Elongation competent ribosome in complex with bS1
+Macromolecule #1: 16S ribosomal RNA
+Macromolecule #22: P-site fMet-tRNA(fMet)
+Macromolecule #23: E-site tRNA
+Macromolecule #24: mRNA
+Macromolecule #26: 23S ribosomal RNA
+Macromolecule #27: 5S ribosomal RNA
+Macromolecule #2: 30S ribosomal protein S2
+Macromolecule #3: 30S ribosomal protein S3
+Macromolecule #4: 30S ribosomal protein S4
+Macromolecule #5: 30S ribosomal protein S5
+Macromolecule #6: 30S ribosomal protein S6
+Macromolecule #7: 30S ribosomal protein S7
+Macromolecule #8: 30S ribosomal protein S8
+Macromolecule #9: 30S ribosomal protein S9
+Macromolecule #10: 30S ribosomal protein S10
+Macromolecule #11: 30S ribosomal protein S11
+Macromolecule #12: 30S ribosomal protein S12
+Macromolecule #13: 30S ribosomal protein S13
+Macromolecule #14: 30S ribosomal protein S14
+Macromolecule #15: 30S ribosomal protein S15
+Macromolecule #16: 30S ribosomal protein S16
+Macromolecule #17: 30S ribosomal protein S17
+Macromolecule #18: 30S ribosomal protein S18
+Macromolecule #19: 30S ribosomal protein S19
+Macromolecule #20: 30S ribosomal protein S20
+Macromolecule #21: 30S ribosomal protein S21
+Macromolecule #25: 30S ribosomal protein S1
+Macromolecule #28: 50S ribosomal protein L2
+Macromolecule #29: 50S ribosomal protein L3
+Macromolecule #30: 50S ribosomal protein L4
+Macromolecule #31: 50S ribosomal protein L5
+Macromolecule #32: 50S ribosomal protein L6
+Macromolecule #33: 50S ribosomal protein L9
+Macromolecule #34: 50S ribosomal protein L13
+Macromolecule #35: 50S ribosomal protein L14
+Macromolecule #36: 50S ribosomal protein L15
+Macromolecule #37: 50S ribosomal protein L16
+Macromolecule #38: 50S ribosomal protein L17
+Macromolecule #39: 50S ribosomal protein L18
+Macromolecule #40: 50S ribosomal protein L19
+Macromolecule #41: 50S ribosomal protein L20
+Macromolecule #42: 50S ribosomal protein L21
+Macromolecule #43: 50S ribosomal protein L22
+Macromolecule #44: 50S ribosomal protein L23
+Macromolecule #45: 50S ribosomal protein L24
+Macromolecule #46: 50S ribosomal protein L25
+Macromolecule #47: 50S ribosomal protein L27
+Macromolecule #48: 50S ribosomal protein L28
+Macromolecule #49: 50S ribosomal protein L29
+Macromolecule #50: 50S ribosomal protein L30
+Macromolecule #51: 50S ribosomal protein L32
+Macromolecule #52: 50S ribosomal protein L33
+Macromolecule #53: 50S ribosomal protein L34
+Macromolecule #54: 50S ribosomal protein L35
+Macromolecule #55: 50S ribosomal protein L36
+Macromolecule #56: 50S ribosomal protein L31
+Macromolecule #57: MAGNESIUM ION
+Macromolecule #58: ZINC ION
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 Component:
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Grid | Model: Quantifoil R3.5/1 / Material: COPPER / Mesh: 200 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 20 sec. | ||||||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 293.15 K / Instrument: FEI VITROBOT MARK III |
-Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Number real images: 6381 / Average electron dose: 35.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.4 µm / Nominal magnification: 36000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Talos Arctica / Image courtesy: FEI Company |