[English] 日本語
Yorodumi- EMDB-17448: Spraguea lophii ribosome in the closed conformation by cryo sub t... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-17448 | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | Spraguea lophii ribosome in the closed conformation by cryo sub tomogram averaging | ||||||||||||
Map data | B-factor -200 is applied for map sharpening. | ||||||||||||
Sample |
| ||||||||||||
Keywords | Microsporidia / RIBOSOME | ||||||||||||
Function / homology | Function and homology information 90S preribosome / translation regulator activity / maturation of LSU-rRNA / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / rescue of stalled ribosome / ribosomal large subunit biogenesis / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / protein kinase C binding / modification-dependent protein catabolic process / protein tag activity ...90S preribosome / translation regulator activity / maturation of LSU-rRNA / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / rescue of stalled ribosome / ribosomal large subunit biogenesis / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / protein kinase C binding / modification-dependent protein catabolic process / protein tag activity / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / ribosome binding / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / ribosomal large subunit assembly / cytoplasmic translation / cytosolic large ribosomal subunit / negative regulation of translation / rRNA binding / ribosome / protein ubiquitination / structural constituent of ribosome / positive regulation of protein phosphorylation / ribonucleoprotein complex / translation / mRNA binding / ubiquitin protein ligase binding / nucleolus / RNA binding / zinc ion binding / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||||||||
Biological species | Spraguea lophii 42_110 (fungus) | ||||||||||||
Method | subtomogram averaging / cryo EM / Resolution: 10.8 Å | ||||||||||||
Authors | Gil Diez P / McLaren M / Isupov MN / Daum B / Conners R / Williams B | ||||||||||||
Funding support | United Kingdom, 1 items
| ||||||||||||
Citation | Journal: Nat Microbiol / Year: 2023 Title: CryoEM reveals that ribosomes in microsporidian spores are locked in a dimeric hibernating state. Authors: Mathew McLaren / Rebecca Conners / Michail N Isupov / Patricia Gil-Díez / Lavinia Gambelli / Vicki A M Gold / Andreas Walter / Sean R Connell / Bryony Williams / Bertram Daum / Abstract: Translational control is an essential process for the cell to adapt to varying physiological or environmental conditions. To survive adverse conditions such as low nutrient levels, translation can be ...Translational control is an essential process for the cell to adapt to varying physiological or environmental conditions. To survive adverse conditions such as low nutrient levels, translation can be shut down almost entirely by inhibiting ribosomal function. Here we investigated eukaryotic hibernating ribosomes from the microsporidian parasite Spraguea lophii in situ by a combination of electron cryo-tomography and single-particle electron cryo-microscopy. We show that microsporidian spores contain hibernating ribosomes that are locked in a dimeric (100S) state, which is formed by a unique dimerization mechanism involving the beak region. The ribosomes within the dimer are fully assembled, suggesting that they are ready to be activated once the host cell is invaded. This study provides structural evidence for dimerization acting as a mechanism for ribosomal hibernation in microsporidia, and therefore demonstrates that eukaryotes utilize this mechanism in translational control. | ||||||||||||
History |
|
-Structure visualization
Supplemental images |
---|
-Downloads & links
-EMDB archive
Map data | emd_17448.map.gz | 656.7 KB | EMDB map data format | |
---|---|---|---|---|
Header (meta data) | emd-17448-v30.xml emd-17448.xml | 93.3 KB 93.3 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_17448_fsc.xml | 3.7 KB | Display | FSC data file |
Images | emd_17448.png | 50.7 KB | ||
Filedesc metadata | emd-17448.cif.gz | 17.7 KB | ||
Others | emd_17448_half_map_1.map.gz emd_17448_half_map_2.map.gz | 2.8 MB 2.8 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-17448 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-17448 | HTTPS FTP |
-Validation report
Summary document | emd_17448_validation.pdf.gz | 762.8 KB | Display | EMDB validaton report |
---|---|---|---|---|
Full document | emd_17448_full_validation.pdf.gz | 762.4 KB | Display | |
Data in XML | emd_17448_validation.xml.gz | 9.4 KB | Display | |
Data in CIF | emd_17448_validation.cif.gz | 12.3 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17448 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17448 | HTTPS FTP |
-Related structure data
Related structure data | 8p5dMC 8p60C 16198 M: atomic model generated by this map C: citing same article (ref.) |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
---|---|
Related items in Molecule of the Month |
-Map
File | Download / File: emd_17448.map.gz / Format: CCP4 / Size: 3.8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | B-factor -200 is applied for map sharpening. | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 4.53 Å | ||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Half map: #1
File | emd_17448_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #2
File | emd_17448_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Sample components
+Entire : Ribosome
+Supramolecule #1: Ribosome
+Macromolecule #1: RNA 28S
+Macromolecule #2: RNA 5S
+Macromolecule #42: RNA 16S
+Macromolecule #3: 60S ribosomal protein L8
+Macromolecule #4: uL15
+Macromolecule #5: 60S ribosomal protein L3
+Macromolecule #6: 60S ribosomal protein L4
+Macromolecule #7: 60S ribosomal protein L3
+Macromolecule #8: 60S ribosomal protein L5
+Macromolecule #9: 60S ribosomal protein L31
+Macromolecule #10: 60S ribosomal protein L6
+Macromolecule #11: 60S ribosomal protein L32
+Macromolecule #12: 60S ribosomal protein L7
+Macromolecule #13: 60S ribosomal protein L35a
+Macromolecule #14: 60S ribosomal protein L8
+Macromolecule #15: Ribosomal protein L34
+Macromolecule #16: 60S ribosomal protein L9
+Macromolecule #17: Ribosomal L29 protein (Fragment),Ribosomal L29 protein (Fragment)...
+Macromolecule #18: S60 ribosomal protein L10
+Macromolecule #19: 60S ribosomal protein L36
+Macromolecule #20: 60S ribosomal protein L11
+Macromolecule #21: eL37
+Macromolecule #22: 60S ribosomal protein L13
+Macromolecule #23: 60S ribosomal protein L39
+Macromolecule #24: Transposase
+Macromolecule #25: Ubiquitin
+Macromolecule #26: Ribosomal protein L15
+Macromolecule #27: Ribosomal protein L13A
+Macromolecule #28: 60S ribosomal protein L44
+Macromolecule #29: 60S ribosomal protein L17
+Macromolecule #30: 60S ribosomal protein L37a
+Macromolecule #31: 60S ribosomal protein L18
+Macromolecule #32: 60S ribosomal protein L19
+Macromolecule #33: 60S ribosomal protein L20
+Macromolecule #34: 60s ribosomal protein L21
+Macromolecule #35: 60S ribosomal protein L22
+Macromolecule #36: Ribosomal protein L23
+Macromolecule #37: Ribosomal protein L24E
+Macromolecule #38: 60S ribosomal protein L23a
+Macromolecule #39: 60S ribosomal protein L26
+Macromolecule #40: 60S ribosomal protein L27
+Macromolecule #41: DNL-type domain-containing protein
+Macromolecule #43: 40S ribosomal protein S0
+Macromolecule #44: 40S ribosomal protein S26
+Macromolecule #45: eS1
+Macromolecule #46: eS27
+Macromolecule #47: 40S ribosomal protein S2
+Macromolecule #48: eS28
+Macromolecule #49: 40S ribosomal protein S3
+Macromolecule #50: 40S ribosomal protein S29
+Macromolecule #51: 40S ribosomal protein S4
+Macromolecule #52: eS30
+Macromolecule #53: 40S ribosomal protein S5
+Macromolecule #54: Ubiquitin/40s ribosomal protein S27a fusion
+Macromolecule #55: 40S ribosomal protein S6
+Macromolecule #56: Guanine nucleotide binding protein beta subunit
+Macromolecule #57: 40S ribosomal protein S7
+Macromolecule #58: 40S ribosomal protein S8
+Macromolecule #59: 40S ribosomal protein S9
+Macromolecule #60: 40S ribosomal protein S10
+Macromolecule #61: 40S ribosomal protein S11
+Macromolecule #62: 40S ribosomal protein S12
+Macromolecule #63: 40S ribosomal protein S13
+Macromolecule #64: 40S ribosomal protein S14
+Macromolecule #65: Ribosomal protein S19
+Macromolecule #66: 40S ribosomal protein S16
+Macromolecule #67: eS17
+Macromolecule #68: 40S ribosomal protein S18
+Macromolecule #69: 40S Ribosomal protein S19
+Macromolecule #70: 40S ribosomal protein S20
+Macromolecule #71: Ribosomal protein S21E
+Macromolecule #72: 40S ribosomal protein S15A
+Macromolecule #73: uS12
+Macromolecule #74: 40s ribosomal protein s24
+Macromolecule #75: 40S ribosomal protein S25
+Macromolecule #76: ZINC ION
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
Processing | subtomogram averaging |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
---|---|
Grid | Model: Quantifoil / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 2 / Details: 20 mA, Carbon coated grid |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 288.15 K / Instrument: FEI VITROBOT MARK IV / Details: blot force -1 and blot time 4 s. |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Image recording | #0 - Image recording ID: 1 / #0 - Film or detector model: GATAN K2 SUMMIT (4k x 4k) / #0 - Detector mode: COUNTING / #0 - Average electron dose: 1.98 e/Å2 / #1 - Image recording ID: 2 / #1 - Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / #1 - Average electron dose: 1.98 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 6.0 µm / Nominal defocus min: 2.5 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Refinement | Space: REAL / Protocol: RIGID BODY FIT |
---|---|
Output model | PDB-8p5d: |