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Yorodumi- EMDB-36331: Atomic structure of wheat ribosome reveals unique features of the... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-36331 | |||||||||
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Title | Atomic structure of wheat ribosome reveals unique features of the plant ribosomes | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Protein Synthesis Machinery / Eukaryotic Ribosome / Plant / TRANSLATION / RIBOSOME | |||||||||
Function / homology | Function and homology information protein-RNA complex assembly / maturation of LSU-rRNA / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / ribosome biogenesis / large ribosomal subunit rRNA binding / 5S rRNA binding / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit ...protein-RNA complex assembly / maturation of LSU-rRNA / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / ribosome biogenesis / large ribosomal subunit rRNA binding / 5S rRNA binding / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / mRNA binding / RNA binding / nucleus / metal ion binding / cytoplasm Similarity search - Function | |||||||||
Biological species | Triticum aestivum (bread wheat) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.84 Å | |||||||||
Authors | Mishra RK / Sharma P / Hussain T | |||||||||
Funding support | United Kingdom, 1 items
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Citation | Journal: Structure / Year: 2024 Title: Cryo-EM structure of wheat ribosome reveals unique features of the plant ribosomes. Authors: Rishi Kumar Mishra / Prafful Sharma / Faisal Tarique Khaja / Adwaith B Uday / Tanweer Hussain / Abstract: Plants being sessile organisms exhibit unique features in ribosomes, which might aid in rapid gene expression and regulation in response to varying environmental conditions. Here, we present high- ...Plants being sessile organisms exhibit unique features in ribosomes, which might aid in rapid gene expression and regulation in response to varying environmental conditions. Here, we present high-resolution structures of the 60S and 80S ribosomes from wheat, a monocot staple crop plant (Triticum aestivum). While plant ribosomes have unique plant-specific rRNA modification (Cm1847) in the peptide exit tunnel (PET), the zinc-finger motif in eL34 is absent, and uL4 is extended, making an exclusive interaction network. We note differences in the eL15-helix 11 (25S) interaction, eL6-ES7 assembly, and certain rRNA chemical modifications between monocot and dicot ribosomes. In eukaryotes, we observe highly conserved rRNA modification (Gm75) in 5.8S rRNA and a flipped base (G1506) in PET. These features are likely involved in sensing or stabilizing nascent chain. Finally, we discuss the importance of the universal conservation of three consecutive rRNA modifications in all ribosomes for their interaction with A-site aminoacyl-tRNA. #1: Journal: Acta Crystallogr., Sect. D: Biol. Crystallogr. / Year: 2018 Title: Real-space refinement in PHENIX for cryo-EM and crystallography Authors: Uday AB / Khaja FT | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_36331.map.gz | 166.4 MB | EMDB map data format | |
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Header (meta data) | emd-36331-v30.xml emd-36331.xml | 63 KB 63 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_36331_fsc.xml | 12.7 KB | Display | FSC data file |
Images | emd_36331.png | 49.7 KB | ||
Filedesc metadata | emd-36331.cif.gz | 14 KB | ||
Others | emd_36331_half_map_1.map.gz emd_36331_half_map_2.map.gz | 138 MB 138 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-36331 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-36331 | HTTPS FTP |
-Validation report
Summary document | emd_36331_validation.pdf.gz | 969.5 KB | Display | EMDB validaton report |
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Full document | emd_36331_full_validation.pdf.gz | 969 KB | Display | |
Data in XML | emd_36331_validation.xml.gz | 20.3 KB | Display | |
Data in CIF | emd_36331_validation.cif.gz | 26.5 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-36331 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-36331 | HTTPS FTP |
-Related structure data
Related structure data | 8jivMC 8jiwC 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_36331.map.gz / Format: CCP4 / Size: 178 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: 1.07 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_36331_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_36331_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
+Entire : The large subunit of wheat Ribosome
+Supramolecule #1: The large subunit of wheat Ribosome
+Macromolecule #1: 25S rRNA
+Macromolecule #2: 5S rRNA
+Macromolecule #3: 5.8S rRNA
+Macromolecule #4: Ribosomal protein L2 C-terminal domain-containing protein
+Macromolecule #5: Ribosomal protein L3
+Macromolecule #6: 60S ribosomal protein L4 C-terminal domain-containing protein
+Macromolecule #7: Ribosomal protein L5 eukaryotic C-terminal domain-containing protein
+Macromolecule #8: 60S ribosomal protein L6
+Macromolecule #9: 60S ribosomal protein uL30
+Macromolecule #10: 60S ribosomal protein L7a
+Macromolecule #11: Ribosomal protein L6 alpha-beta domain-containing protein
+Macromolecule #12: Ribosomal protein L10e/L16 domain-containing protein
+Macromolecule #13: 60S ribosomal protein L11
+Macromolecule #14: 60S ribosomal protein L13
+Macromolecule #15: Ribosomal protein L14e domain-containing protein
+Macromolecule #16: Ribosomal protein L15
+Macromolecule #17: Ribosomal protein L13a
+Macromolecule #18: 60S ribosomal protein uL22
+Macromolecule #19: Ribosomal protein L18e/L15P domain-containing protein
+Macromolecule #20: Ribosomal protein L19
+Macromolecule #21: 60S ribosomal protein L18a
+Macromolecule #22: 60S ribosomal protein L21
+Macromolecule #23: Genome assembly, chromosome: II
+Macromolecule #24: Ribosomal protein L17
+Macromolecule #25: TRASH domain-containing protein
+Macromolecule #26: Genome assembly, chromosome: II
+Macromolecule #27: KOW domain-containing protein
+Macromolecule #28: 60S ribosomal protein L27
+Macromolecule #29: Ribosomal protein L18e/L15P domain-containing protein
+Macromolecule #30: 60S ribosomal protein L29
+Macromolecule #31: Ribosomal protein L7Ae/L30e/S12e/Gadd45 domain-containing protein
+Macromolecule #32: 60S ribosomal protein L31
+Macromolecule #33: 60S ribosomal protein eL32
+Macromolecule #34: 60S ribosomal protein eL33
+Macromolecule #35: 60S ribosomal protein L34
+Macromolecule #36: 60S ribosomal protein L35
+Macromolecule #37: 60S ribosomal protein L36
+Macromolecule #38: Ribosomal protein L37
+Macromolecule #39: 60S ribosomal protein L38
+Macromolecule #40: Ribosomal protein L39
+Macromolecule #41: Ubiquitin-like domain-containing protein
+Macromolecule #42: Genome assembly, chromosome: II
+Macromolecule #43: 60S ribosomal protein L37a, expressed
+Macromolecule #44: Ribosomal L28e/Mak16 domain-containing protein
+Macromolecule #45: POTASSIUM ION
+Macromolecule #46: MAGNESIUM ION
+Macromolecule #47: ZINC ION
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.6 |
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Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 400 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 289 K / Instrument: FEI VITROBOT MARK IV |
Details | The sample is the large subunit of wheat ribosome |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 44.6 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 2.7 µm / Calibrated magnification: 75000 / Illumination mode: OTHER / Imaging mode: OTHER / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.5 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |