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- EMDB-37604: Structural basis of translation inhibition by a valine tRNA-deriv... -
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Open data
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Basic information
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Title | Structural basis of translation inhibition by a valine tRNA-derived fragment | |||||||||
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![]() | Sulfolobus acidocaldarius ribosome / RIBOSOME | |||||||||
Function / homology | ![]() ribonuclease P activity / tRNA 5'-leader removal / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / ribosome biogenesis / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit ...ribonuclease P activity / tRNA 5'-leader removal / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / ribosome biogenesis / 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 / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / RNA binding / zinc ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.62 Å | |||||||||
![]() | Wang YH / Zhou J | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis of translation inhibition by a valine tRNA-derived fragment. Authors: Yun Wu / Meng-Ting Ni / Ying-Hui Wang / Chen Wang / Hai Hou / Xing Zhang / Jie Zhou / ![]() Abstract: Translational regulation by non-coding RNAs is a mechanism commonly used by cells to fine-tune gene expression. A fragment derived from an archaeal valine tRNA (Val-tRF) has been previously ...Translational regulation by non-coding RNAs is a mechanism commonly used by cells to fine-tune gene expression. A fragment derived from an archaeal valine tRNA (Val-tRF) has been previously identified to bind the small subunit of the ribosome and inhibit translation in Here, we present three cryo-electron microscopy structures of Val-tRF bound to the small subunit of ribosomes at resolutions between 4.02 and 4.53 Å. Within these complexes, Val-tRF was observed to bind to conserved RNA-interacting sites, including the ribosomal decoding center. The binding of Val-tRF destabilizes helices h24, h44, and h45 and the anti-Shine-Dalgarno sequence of 16S rRNA. The binding position of this molecule partially overlaps with the translation initiation factor aIF1A and occludes the mRNA P-site codon. Moreover, we found that the binding of Val-tRF is associated with steric hindrance of the H69 base of 23S rRNA in the large ribosome subunit, thereby preventing 70S assembly. Our data exemplify how tRNA-derived fragments bind to ribosomes and provide new insights into the mechanisms underlying translation inhibition by Val-tRFs. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 51.3 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 46.4 KB 46.4 KB | Display Display | ![]() |
Images | ![]() | 111 KB | ||
Filedesc metadata | ![]() | 9.5 KB | ||
Others | ![]() ![]() | 95.5 MB 95.5 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 881.5 KB | Display | ![]() |
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Full document | ![]() | 881.1 KB | Display | |
Data in XML | ![]() | 13.6 KB | Display | |
Data in CIF | ![]() | 16.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8wkpMC ![]() 8wq2C ![]() 8wq4C M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.087 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_37604_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_37604_half_map_2.map | ||||||||||||
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Density Histograms |
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Sample components
+Entire : Sulfolobus acidocaldarius ribosome
+Supramolecule #1: Sulfolobus acidocaldarius ribosome
+Macromolecule #1: RNA (1328-MER)
+Macromolecule #2: RNA (25-MER)
+Macromolecule #3: 30S ribosomal protein S2
+Macromolecule #4: 30S ribosomal protein S4e
+Macromolecule #5: 30S ribosomal protein S4
+Macromolecule #6: 30S ribosomal protein S5
+Macromolecule #7: 30S ribosomal protein S6e
+Macromolecule #8: 30S ribosomal protein S8e
+Macromolecule #9: 30S ribosomal protein S11
+Macromolecule #10: 30S ribosomal protein S12
+Macromolecule #11: 30S ribosomal protein S15
+Macromolecule #12: 30S ribosomal protein S17
+Macromolecule #13: 30S ribosomal protein S24e
+Macromolecule #14: 30S ribosomal protein S27e
+Macromolecule #15: 30S ribosomal protein S3Ae
+Macromolecule #16: 30S ribosomal protein S3
+Macromolecule #17: 30S ribosomal protein S7
+Macromolecule #18: 30S ribosomal protein S9
+Macromolecule #19: 30S ribosomal protein S10
+Macromolecule #20: 30S ribosomal protein S13
+Macromolecule #21: 30S ribosomal protein S14 type Z
+Macromolecule #22: 30S ribosomal protein S17e
+Macromolecule #23: 30S ribosomal protein S19e
+Macromolecule #24: 30S ribosomal protein S19
+Macromolecule #25: 30S ribosomal protein S28e
+Macromolecule #26: 50S ribosomal protein L7Ae
+Macromolecule #27: 30S ribosomal protein S27ae
+Macromolecule #28: Small ribosomal subunit protein uS8
+Macromolecule #29: UNKNOWN LIGAND
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | 2D array |
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Sample preparation
Concentration | 5 mg/mL |
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Buffer | pH: 7.5 |
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 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 26.7 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: PDB ENTRY PDB model - PDB ID: |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.62 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 5357 |
Initial angle assignment | Type: NOT APPLICABLE |
Final angle assignment | Type: NOT APPLICABLE |