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Yorodumi- EMDB-73602: Babesia divergens ribosome structure by single-particle cryo-EM (... -
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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Babesia divergens ribosome structure by single-particle cryo-EM (3D class1, A-, P-, and E-site tRNAs and mRNA) | |||||||||
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Sample |
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Keywords | tRNAs / RNA modification / 80S / RIBOSOME | |||||||||
| Function / homology | Function and homology informationpreribosome / 90S preribosome / protein-RNA complex assembly / translation regulator activity / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / chloroplast / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / small-subunit processome ...preribosome / 90S preribosome / protein-RNA complex assembly / translation regulator activity / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / chloroplast / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / small-subunit processome / kinase activity / rRNA processing / large ribosomal subunit / ribosomal small subunit assembly / ribosome biogenesis / ribosome binding / ribosomal small subunit biogenesis / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / cytoplasmic translation / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / nucleolus / RNA binding / zinc ion binding / nucleus / cytoplasm / cytosol Similarity search - Function | |||||||||
| Biological species | Babesia divergens (eukaryote) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.1 Å | |||||||||
Authors | Gutierrez-Vargas C / Izhaki-Tavor LS / Leger-Abraham M | |||||||||
| Funding support | United States, 2 items
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Citation | Journal: To Be PublishedTitle: Ribosomal architecture and rRNA modification landscape in the tick-borne parasite Babesia divergens Authors: Gutierrez-Vargas C / Izhaki-Tavor LS / Calvopina-Chavez D / Keroack C / Copello P / Duraisingh M / Leger-Abraham M | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_73602.map.gz | 307.4 MB | EMDB map data format | |
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| Header (meta data) | emd-73602-v30.xml emd-73602.xml | 121.8 KB 121.8 KB | Display Display | EMDB header |
| Images | emd_73602.png | 125.4 KB | ||
| Filedesc metadata | emd-73602.cif.gz | 20.6 KB | ||
| Others | emd_73602_additional_1.map.gz | 36.9 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-73602 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-73602 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9yxbMC ![]() 9ygmC 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_73602.map.gz / Format: CCP4 / Size: 343 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: 0.825 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Additional map: #1
| File | emd_73602_additional_1.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
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Sample components
+Entire : 80S ribosome
+Supramolecule #1: 80S ribosome
+Supramolecule #2: 40S
+Supramolecule #3: 60S
+Macromolecule #1: 40S ribosomal protein uS12
+Macromolecule #2: 40S ribosomal protein eS19
+Macromolecule #3: 40S ribosomal protein uS17
+Macromolecule #4: 40S ribosomal protein uS9
+Macromolecule #5: 40S ribosomal protein uS13
+Macromolecule #6: 40S ribosomal protein uS7
+Macromolecule #7: 40S ribosomal protein uS15
+Macromolecule #8: 40S ribosomal protein eS1
+Macromolecule #9: 40S ribosomal protein eS10
+Macromolecule #10: 40S ribosomal protein uS8
+Macromolecule #11: 40S ribosomal protein eS7
+Macromolecule #12: 40S ribosomal protein eS8
+Macromolecule #13: 40S ribosomal protein eS6
+Macromolecule #14: 40S ribosomal protein uS10
+Macromolecule #15: 40S ribosomal protein eS30
+Macromolecule #16: 40S ribosomal protein uS14
+Macromolecule #17: 40S ribosomal protein eS28
+Macromolecule #18: 40S ribosomal protein uS3
+Macromolecule #19: 40S ribosomal protein uS19
+Macromolecule #20: 40S ribosomal protein uS2
+Macromolecule #21: 40S ribosomal protein uS5
+Macromolecule #22: 40S ribosomal protein eS26
+Macromolecule #23: 40S ribosomal protein eS17
+Macromolecule #24: 40S ribosomal protein uS11
+Macromolecule #25: 40S ribosomal protein eS24
+Macromolecule #26: 40S ribosomal protein eS25
+Macromolecule #27: 40S ribosomal protein eS12
+Macromolecule #28: 40S ribosomal protein uS4
+Macromolecule #29: 40S ribosomal protein eS31
+Macromolecule #30: 40S ribosomal protein eS27
+Macromolecule #32: 60S ribosomal protein uL15
+Macromolecule #33: 60S ribosomal protein eL20
+Macromolecule #34: 60S ribosomal protein eL31
+Macromolecule #35: 60S ribosomal protein eL32
+Macromolecule #36: 60S ribosomal protein eL37
+Macromolecule #37: 60S ribosomal protein eL18
+Macromolecule #38: 60S ribosomal protein uL2
+Macromolecule #39: 60S ribosomal protein uL13
+Macromolecule #40: 60S ribosomal protein eL13
+Macromolecule #41: 60S ribosomal protein uL24
+Macromolecule #42: 60S ribosomal protein uL29
+Macromolecule #43: 60S ribosomal protein uL4
+Macromolecule #44: 60S ribosomal protein uL18
+Macromolecule #45: 60S ribosomal protein eL27
+Macromolecule #46: 60S ribosomal protein uL22
+Macromolecule #47: 60S ribosomal protein eL8
+Macromolecule #48: 60S ribosomal protein uL3
+Macromolecule #49: 60S ribosomal protein eL14
+Macromolecule #50: 60S ribosomal protein uL14
+Macromolecule #51: 60S ribosomal protein uL23
+Macromolecule #52: 60S ribosomal protein eL36
+Macromolecule #53: 60S ribosomal protein eL40
+Macromolecule #54: 60S ribosomal protein eL21
+Macromolecule #55: 60S ribosomal protein eL42
+Macromolecule #56: 60S ribosomal protein eL39
+Macromolecule #57: 60S ribosomal protein eL19
+Macromolecule #58: 60S ribosomal protein uL5
+Macromolecule #59: 60S ribosomal protein uL16
+Macromolecule #60: 60S ribosomal protein eL15
+Macromolecule #61: 60S ribosomal protein eL33
+Macromolecule #62: 60S ribosomal protein uL30
+Macromolecule #63: 60S ribosomal protein eL22
+Macromolecule #64: 60S ribosomal protein eL30
+Macromolecule #65: 60S ribosomal protein eL43
+Macromolecule #66: 60S ribosomal protein eL29
+Macromolecule #67: 60S ribosomal protein eL34
+Macromolecule #68: 60S ribosomal protein eL24
+Macromolecule #69: 60S ribosomal protein eL6
+Macromolecule #70: 60S ribosomal protein eL41
+Macromolecule #78: 40S ribosomal protein eS21
+Macromolecule #79: 40S ribosomal protein eS4
+Macromolecule #80: Receptor for activated C kinase 1, RACK1 protein
+Macromolecule #81: 60S ribosomal protein uL6
+Macromolecule #82: 60S ribosomal protein eL38
+Macromolecule #31: 18S ribosomal RNA
+Macromolecule #71: 5S ribosomal RNA
+Macromolecule #72: 5.8S ribosomal RNA
+Macromolecule #73: 28S ribosomal RNA
+Macromolecule #74: E-site tRNA
+Macromolecule #75: P-site tRNA
+Macromolecule #76: A-site tRNA
+Macromolecule #77: mRNA fragment
+Macromolecule #83: MAGNESIUM ION
+Macromolecule #84: POTASSIUM 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 Component:
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| Grid | Model: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Support film - Film thickness: 12 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.037 kPa Details: The grid had an additional ultrathin continous carbon layer (2 nm) | ||||||||||||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Software | Name: EPU |
| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number real images: 12144 / Average exposure time: 1.4 sec. / Average electron dose: 42.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.2 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 105000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model |
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| Details | Protein chains were built de novo with ModelAngelo. The rRNA chains from PDB 9YGM, which corresponds to the highest-resolution conformational class (3DC3, 80S with E-site tRNA) from the same dataset, were rigid-body fit and remodeled. The complete model then underwent iterative rounds of manual adjustment in Coot and real-space refinement in Phenix. | ||||||||||||||||||
| Refinement | Space: REAL / Protocol: RIGID BODY FIT | ||||||||||||||||||
| Output model | ![]() PDB-9yxb: |
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About Yorodumi



Keywords
Babesia divergens (eukaryote)
Authors
United States, 2 items
Citation













Z (Sec.)
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FIELD EMISSION GUN
