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Yorodumi- EMDB-72933: 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 class3, E-site tRNA) | |||||||||
Map data | ||||||||||
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: 2.7 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_72933.map.gz | 303.9 MB | EMDB map data format | |
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| Header (meta data) | emd-72933-v30.xml emd-72933.xml | 110.3 KB 110.3 KB | Display Display | EMDB header |
| Images | emd_72933.png | 124.7 KB | ||
| Filedesc metadata | emd-72933.cif.gz | 21 KB | ||
| Others | emd_72933_additional_1.map.gz | 37.6 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-72933 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-72933 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9ygmMC ![]() 9yxbC M: atomic model generated by this map C: citing same article ( |
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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_72933.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_72933_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
+Macromolecule #1: 5S ribosomal RNA
+Macromolecule #73: 5.8S ribosomal RNA
+Macromolecule #74: 28S ribosomal RNA
+Macromolecule #75: E-site tRNA
+Macromolecule #76: 18S ribosomal RNA
+Macromolecule #2: 60S ribosomal protein uL2
+Macromolecule #3: 60S ribosomal protein uL3
+Macromolecule #4: 60S ribosomal protein uL5
+Macromolecule #5: 60S ribosomal protein uL6
+Macromolecule #6: 60S ribosomal protein eL6
+Macromolecule #7: 60S ribosomal protein eL13
+Macromolecule #8: 60S ribosomal protein uL14
+Macromolecule #9: 60S ribosomal protein uL18
+Macromolecule #10: 60S ribosomal protein eL18
+Macromolecule #11: 60S ribosomal protein uL22
+Macromolecule #12: 60S ribosomal protein eL22
+Macromolecule #13: 60S ribosomal protein eL27
+Macromolecule #14: 60S ribosomal protein uL29
+Macromolecule #15: 60S ribosomal protein eL29
+Macromolecule #16: 60S ribosomal protein eL30
+Macromolecule #17: 60S ribosomal protein eL31
+Macromolecule #18: 60S ribosomal protein eL32
+Macromolecule #19: 60S ribosomal protein eL33
+Macromolecule #20: 60S ribosomal protein uL4
+Macromolecule #21: 60S ribosomal protein uL13
+Macromolecule #22: 60S ribosomal protein eL14
+Macromolecule #23: 60S ribosomal protein uL15
+Macromolecule #24: 60S ribosomal protein eL15
+Macromolecule #25: 60S ribosomal protein uL16
+Macromolecule #26: 60S ribosomal protein eL19
+Macromolecule #27: 60S ribosomal protein eL20
+Macromolecule #28: 60S ribosomal protein eL21
+Macromolecule #29: 60S ribosomal protein uL24
+Macromolecule #30: 60S ribosomal protein uL30
+Macromolecule #31: 60S ribosomal protein eL34
+Macromolecule #32: 60S ribosomal protein eL36
+Macromolecule #33: 60S ribosomal protein eL37
+Macromolecule #34: 60S ribosomal protein eL38
+Macromolecule #35: 60S ribosomal protein eL39
+Macromolecule #36: 60S ribosomal protein eL40
+Macromolecule #37: 60S ribosomal protein eL43
+Macromolecule #38: 60S ribosomal protein eL42
+Macromolecule #39: 60S ribosomal protein eL8
+Macromolecule #40: 40S ribosomal protein eS1
+Macromolecule #41: 40S ribosomal protein uS2
+Macromolecule #42: 40S ribosomal protein uS4
+Macromolecule #43: 40S ribosomal protein eS4
+Macromolecule #44: 40S ribosomal protein uS5
+Macromolecule #45: 40S ribosomal protein eS6
+Macromolecule #46: 40S ribosomal protein eS7
+Macromolecule #47: 40S ribosomal protein uS8
+Macromolecule #48: 40S ribosomal protein eS8
+Macromolecule #49: 40S ribosomal protein uS12
+Macromolecule #50: 40S ribosomal protein uS15
+Macromolecule #51: 40S ribosomal protein uS17
+Macromolecule #52: 40S ribosomal protein eS21
+Macromolecule #53: 40S ribosomal protein eS26
+Macromolecule #54: 40S ribosomal protein eS27
+Macromolecule #55: 40S ribosomal protein eS30
+Macromolecule #56: 40S ribosomal protein uS3
+Macromolecule #57: 40S ribosomal protein uS7
+Macromolecule #58: 40S ribosomal protein uS9
+Macromolecule #59: 40S ribosomal protein uS10
+Macromolecule #60: 40S ribosomal protein eS12
+Macromolecule #61: 40S ribosomal protein uS13
+Macromolecule #62: 40S ribosomal protein uS14
+Macromolecule #63: 40S ribosomal protein uS19
+Macromolecule #64: 40S ribosomal protein eS28
+Macromolecule #65: Receptor for activated C kinase 1, RACK1 protein
+Macromolecule #66: 40S ribosomal protein eS10
+Macromolecule #67: 40S ribosomal protein eS24
+Macromolecule #68: 40S ribosomal protein eS25
+Macromolecule #69: 40S ribosomal protein eS31
+Macromolecule #70: 60S ribosomal protein eL41
+Macromolecule #71: 40S ribosomal protein eS17
+Macromolecule #72: 40S ribosomal protein uS11
+Macromolecule #77: 60S ribosomal protein uL1
+Macromolecule #78: 60S ribosomal protein uL23
+Macromolecule #79: 60S ribosomal protein eL24
+Macromolecule #80: 40S ribosomal protein eS19
+Macromolecule #81: MAGNESIUM ION
+Macromolecule #82: ZINC ION
+Macromolecule #83: POTASSIUM ION
+Macromolecule #84: water
-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 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.037 kPa Details: The grid had an additional ultrathin continuous 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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| 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 | Initial docking and fitting was done in UCSF ChimeraX for the ribosomal proteins using AlphaFold2 predicted models, except for eL41; the T. gondii eL41 chain (PDB 5XXB) served as the initial model. The T. gondii PDBs 5XXU and 5XXB were also fit with UCSF ChimeraX and used for initial model building of the Babesia divergens rRNAs. | ||||||||||||||||||||||||
| Refinement | Protocol: RIGID BODY FIT | ||||||||||||||||||||||||
| Output model | ![]() PDB-9ygm: |
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About Yorodumi



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


















Z (Sec.)
Y (Row.)
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FIELD EMISSION GUN



