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- EMDB-47628: Cryo-EM structure of the Pyrobaculum calidifontis 70S ribosome (C... -
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Open data
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Basic information
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Title | Cryo-EM structure of the Pyrobaculum calidifontis 70S ribosome (Composite Map) | |||||||||
![]() | Pyrobaculum calidifontis 70S ribosome (composite map) | |||||||||
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![]() | Ribosome / Translation / Hibernation / RNA | |||||||||
Function / homology | ![]() ribonuclease P activity / tRNA 5'-leader removal / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosome biogenesis / large ribosomal subunit / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit ...ribonuclease P activity / tRNA 5'-leader removal / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosomal large subunit biogenesis / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosome biogenesis / large ribosomal subunit / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / small ribosomal subunit rRNA binding / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / RNA binding / zinc ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.36 Å | |||||||||
![]() | Nissley AJ / Cate JHD | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of an archaeal ribosome reveals a divergent active site and hibernation factor. Authors: Amos J Nissley / Yekaterina Shulgina / Roan W Kivimae / Blake E Downing / Petar I Penev / Jillian F Banfield / Dipti D Nayak / Jamie H D Cate / ![]() ![]() Abstract: Ribosomes translate mRNA into protein. Despite divergence in ribosome structure over the course of evolution, the catalytic site, known as the peptidyl transferase centre (PTC), is thought to be ...Ribosomes translate mRNA into protein. Despite divergence in ribosome structure over the course of evolution, the catalytic site, known as the peptidyl transferase centre (PTC), is thought to be nearly universally conserved. Here we identify clades of archaea that have highly divergent ribosomal RNA sequences in the PTC. To understand how these PTC sequences fold, we determined cryo-EM structures of the 70S and 50S ribosomes to 2.4 Å and 2 Å, respectively, from the hyperthermophilic archaeon Pyrobaculum calidifontis. PTC sequence variation leads to the rearrangement of key base triples, and differences between archaeal and bacterial ribosomal proteins enable sequence variation in archaeal PTCs. Finally, we identify an archaeal ribosome hibernation factor, Dri, that differs from known bacterial and eukaryotic hibernation factors and is found in multiple archaeal phyla. Overall, this work identifies factors that regulate ribosome function in archaea and reveals a larger diversity of the most ancient sequences in the ribosome. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 744.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 98 KB 98 KB | Display Display | ![]() |
Images | ![]() | 154.6 KB | ||
Filedesc metadata | ![]() | 17.2 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 618.2 KB | Display | ![]() |
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Full document | ![]() | 617.7 KB | Display | |
Data in XML | ![]() | 8.5 KB | Display | |
Data in CIF | ![]() | 9.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9e71MC ![]() 9e6qC ![]() 9e7fC C: citing same article ( M: atomic model generated by this map |
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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
File | ![]() | ||||||||||||||||||||||||||||||||||||
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Annotation | Pyrobaculum calidifontis 70S ribosome (composite map) | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.8293 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
+Entire : 70S ribosome
+Supramolecule #1: 70S ribosome
+Supramolecule #2: 50S Subunit
+Supramolecule #3: 30S subunit
+Macromolecule #1: 5S rRNA
+Macromolecule #2: 23S rRNA
+Macromolecule #3: 16S rRNA
+Macromolecule #4: Large ribosomal subunit protein uL2
+Macromolecule #5: Large ribosomal subunit protein uL3
+Macromolecule #6: Large ribosomal subunit protein uL4
+Macromolecule #7: Large ribosomal subunit protein uL5
+Macromolecule #8: Large ribosomal subunit protein uL6
+Macromolecule #9: Large ribosomal subunit protein eL8
+Macromolecule #10: Large ribosomal subunit protein uL13
+Macromolecule #11: Large ribosomal subunit protein eL13
+Macromolecule #12: Large ribosomal subunit protein uL14
+Macromolecule #13: Large ribosomal subunit protein eL14
+Macromolecule #14: Large ribosomal subunit protein uL15
+Macromolecule #15: 50S ribosomal protein L15e
+Macromolecule #16: Large ribosomal subunit protein uL16
+Macromolecule #17: Large ribosomal subunit protein uL18
+Macromolecule #18: Large ribosomal subunit protein eL18
+Macromolecule #19: Large ribosomal subunit protein eL19
+Macromolecule #20: Large ribosomal subunit protein eL20
+Macromolecule #21: Large ribosomal subunit protein eL21
+Macromolecule #22: Large ribosomal subunit protein uL22
+Macromolecule #23: Large ribosomal subunit protein uL23
+Macromolecule #24: Large ribosomal subunit protein uL24
+Macromolecule #25: Large ribosomal subunit protein eL24
+Macromolecule #26: Large ribosomal subunit protein uL29
+Macromolecule #27: Large ribosomal subunit protein uL30
+Macromolecule #28: Large ribosomal subunit protein eL30
+Macromolecule #29: Large ribosomal subunit protein eL31
+Macromolecule #30: Large ribosomal subunit protein eL32
+Macromolecule #31: Large ribosomal subunit protein eL34
+Macromolecule #32: Large ribosomal subunit protein eL37
+Macromolecule #33: LSU ribosomal protein L38E
+Macromolecule #34: Large ribosomal subunit protein eL39
+Macromolecule #35: Large ribosomal subunit protein eL40
+Macromolecule #36: eL42
+Macromolecule #37: Large ribosomal subunit protein eL43
+Macromolecule #38: DJ-1/PfpI domain-containing protein
+Macromolecule #39: PaREP1 domain containing protein
+Macromolecule #40: Small ribosomal subunit protein eS1
+Macromolecule #41: Small ribosomal subunit protein uS2
+Macromolecule #42: Small ribosomal subunit protein uS3
+Macromolecule #43: Small ribosomal subunit protein uS4
+Macromolecule #44: Small ribosomal subunit protein eS4
+Macromolecule #45: Small ribosomal subunit protein uS5
+Macromolecule #46: Small ribosomal subunit protein eS6
+Macromolecule #47: Small ribosomal subunit protein uS7
+Macromolecule #48: Small ribosomal subunit protein uS8
+Macromolecule #49: Small ribosomal subunit protein eS8
+Macromolecule #50: Small ribosomal subunit protein uS9
+Macromolecule #51: Small ribosomal subunit protein uS10
+Macromolecule #52: Small ribosomal subunit protein uS11
+Macromolecule #53: Small ribosomal subunit protein uS12
+Macromolecule #54: Small ribosomal subunit protein uS13
+Macromolecule #55: Small ribosomal subunit protein uS14
+Macromolecule #56: Small ribosomal subunit protein uS15
+Macromolecule #57: Small ribosomal subunit protein uS17
+Macromolecule #58: Small ribosomal subunit protein eS17
+Macromolecule #59: Small ribosomal subunit protein uS19
+Macromolecule #60: Small ribosomal subunit protein eS19
+Macromolecule #61: Small ribosomal subunit protein eS24
+Macromolecule #62: SSU ribosomal protein S25E
+Macromolecule #63: SSU ribosomal protein S26E
+Macromolecule #64: Small ribosomal subunit protein eS27
+Macromolecule #65: eS28
+Macromolecule #66: SSU ribosomal protein S30E
+Macromolecule #67: aS35
+Macromolecule #68: Small zinc finger protein HVO-2753-like zinc-binding pocket domai...
+Macromolecule #69: SPERMINE
+Macromolecule #70: MAGNESIUM ION
+Macromolecule #71: ZINC ION
+Macromolecule #72: water
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 0.12 mg/mL | ||||||||||||||||||
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Buffer | pH: 7 Component:
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Grid | Model: UltrAuFoil R1.2/1.3 / Material: GOLD / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Pretreatment - Type: GLOW DISCHARGE | ||||||||||||||||||
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 grids imaged: 1 / Number real images: 7318 / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 105000 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Refinement | Protocol: AB INITIO MODEL |
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Output model | ![]() PDB-9e71: |