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Yorodumi- EMDB-55136: Cryo-EM structure of P. abyssi 70S ribosome in complex with hiber... -
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Open data
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Basic information
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| Title | Cryo-EM structure of P. abyssi 70S ribosome in complex with hibernation factor HibA and SBDS | |||||||||
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Keywords | 70S / ribosome / Hibernation / Pyrococcus abyssi | |||||||||
| Function / homology | Function and homology informationribonuclease P activity / tRNA 5'-leader removal / cytosolic ribosome assembly / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / regulation of translation / large ribosomal subunit / ribosomal small subunit assembly ...ribonuclease P activity / tRNA 5'-leader removal / cytosolic ribosome assembly / ribosomal large subunit biogenesis / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / regulation of translation / large ribosomal subunit / ribosomal small subunit assembly / ribosome biogenesis / ribosomal small subunit biogenesis / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / 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 / metal ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() Pyrococcus abyssi GE5 (archaea) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.3 Å | |||||||||
Authors | Madru CM / Bourgeois GB / Mechulam YM / Schmitt ES | |||||||||
| Funding support | France, 1 items
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Citation | Journal: Nat Commun / Year: 2026Title: A family of ribosome hibernation factors widespread in Archaea. Authors: Clément Madru / Gabrielle Bourgeois / Rémi Dulermo / Régine Capeyrou / Gwendoline Joncour / Karima Figuigui / Magalie Duchateau / Julia Chamot-Rooke / Claire Duboc / Stéphane l'Haridon / ...Authors: Clément Madru / Gabrielle Bourgeois / Rémi Dulermo / Régine Capeyrou / Gwendoline Joncour / Karima Figuigui / Magalie Duchateau / Julia Chamot-Rooke / Claire Duboc / Stéphane l'Haridon / Logan Mc Teer / Marta Kwapisz / Béatrice Clouet-d'Orval / Marie Bouvier / Yves Mechulam / Guillaume Borrel / Emmanuelle Schmitt / Didier Flament / ![]() Abstract: Ribosome hibernation preserves translation machinery during stress, yet its mechanisms in Archaea remain poorly defined. Using cryo-EM analysis, we studied hibernation pathways in Pyrococcus abyssi ...Ribosome hibernation preserves translation machinery during stress, yet its mechanisms in Archaea remain poorly defined. Using cryo-EM analysis, we studied hibernation pathways in Pyrococcus abyssi stressed cells. We identified HibA, a previously unrecognized family of hibernation factors widespread in Archaea. HibA consists of a bacterial-like HPF/RaiA domain fused to a Cystathionine Beta Synthase module. Unexpectedly, HibA binds to the ribosome in three different conformations, occupying the A, P and E sites of tRNAs, as well as that of mRNA, enhancing its ability to protect the ribosome from degradation. Idle ribosomes also frequently accumulate the archaeal homolog of eukaryotic ribosome maturation protein SBDS (aSBDS), suggesting that stressed archaeal cells may engage parallel hibernation routes in which aSBDS can complement HibA. Deletion of hibA in Thermococcus barophilus delays recovery from stationary phase and reduces 70S ribosome pools, establishing its role in ribosome preservation. Taxonomic profiling shows that many archaeal lineages encode distinct repertoires of ribosome-associated protection factors, underscoring the modular and multi-layered nature of archaeal hibernation systems. In addition, a comprehensive phylogenetic analysis highlights the evolutionary relationships between prevalent ribosome hibernation factors across Bacteria and Archaea. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Header (meta data) | emd-55136-v30.xml emd-55136.xml | 86.3 KB 86.3 KB | Display Display | EMDB header |
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| FSC (resolution estimation) | emd_55136_fsc.xml | 13.4 KB | Display | FSC data file |
| Images | emd_55136.png | 82.5 KB | ||
| Map data | emd_55136.map.gz | 166.6 MB | EMDB map data format | |
| Filedesc metadata | emd-55136.cif.gz | 16.4 KB | ||
| Others | emd_55136_half_map_1.map.gz emd_55136_half_map_2.map.gz | 43.9 MB 43.9 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-55136 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-55136 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9srbMC ![]() 55135 ![]() 55137 ![]() 55139 ![]() 55636 ![]() 9sraC ![]() 9srcC ![]() 9srdC ![]() 9sreC ![]() 9t7hC 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
-Supplemental data
-Half map: #2
| File | emd_55136_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_55136_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
+Entire : Cryo-EM structure of P. abyssi 70S ribosome in complex with hiber...
+Supramolecule #1: Cryo-EM structure of P. abyssi 70S ribosome in complex with hiber...
+Macromolecule #1: rRNA 23S
+Macromolecule #2: rRNA 16S
+Macromolecule #3: rRNA 5S
+Macromolecule #4: Ribosome maturation protein SDO1 homolog
+Macromolecule #5: Dehydrogenase
+Macromolecule #6: 30S ribosomal protein S3Ae
+Macromolecule #7: 30S ribosomal protein S2
+Macromolecule #8: Zn-ribbon RNA-binding protein involved in translation
+Macromolecule #9: 30S ribosomal protein S4
+Macromolecule #10: 30S ribosomal protein S4e
+Macromolecule #11: 30S ribosomal protein S5
+Macromolecule #12: 30S ribosomal protein S6e
+Macromolecule #13: 30S ribosomal protein S7
+Macromolecule #14: 30S ribosomal protein S8
+Macromolecule #15: 30S ribosomal protein S8e
+Macromolecule #16: 30S ribosomal protein S9
+Macromolecule #17: 30S ribosomal protein S10
+Macromolecule #18: 30S ribosomal protein S11
+Macromolecule #19: 30S ribosomal protein S12
+Macromolecule #20: 30S ribosomal protein S14 type Z
+Macromolecule #21: 30S ribosomal protein S15
+Macromolecule #22: Small ribosomal subunit protein uS17
+Macromolecule #23: 30S ribosomal protein S17e
+Macromolecule #24: 30S ribosomal protein S19e
+Macromolecule #25: 30S ribosomal protein S24e
+Macromolecule #26: 30S ribosomal protein S27e
+Macromolecule #27: 30S ribosomal protein S28e
+Macromolecule #28: 30S ribosomal protein S27ae
+Macromolecule #29: 30S ribosomal protein S3
+Macromolecule #30: Small ribosomal subunit protein eS32
+Macromolecule #31: 50S ribosomal protein L7Ae
+Macromolecule #32: 30S ribosomal protein S19
+Macromolecule #33: 30S ribosomal protein S13
+Macromolecule #34: Large ribosomal subunit protein uL2
+Macromolecule #35: Large ribosomal subunit protein uL30
+Macromolecule #36: Large ribosomal subunit protein uL18
+Macromolecule #37: Large ribosomal subunit protein uL3
+Macromolecule #38: Large ribosomal subunit protein eL14
+Macromolecule #39: Large ribosomal subunit protein uL15
+Macromolecule #40: Large ribosomal subunit protein eL39
+Macromolecule #41: Large ribosomal subunit protein uL24
+Macromolecule #42: Large ribosomal subunit protein eL32
+Macromolecule #43: Large ribosomal subunit protein eL37
+Macromolecule #44: Large ribosomal subunit protein uL5
+Macromolecule #45: Large ribosomal subunit protein eL31
+Macromolecule #46: Large ribosomal subunit protein uL23
+Macromolecule #47: Large ribosomal subunit protein uL29
+Macromolecule #48: Large ribosomal subunit protein eL43
+Macromolecule #49: Large ribosomal subunit protein uL13
+Macromolecule #50: Large ribosomal subunit protein eL21
+Macromolecule #51: Large ribosomal subunit protein eL19
+Macromolecule #52: Large ribosomal subunit protein eL24
+Macromolecule #53: Large ribosomal subunit protein eL42
+Macromolecule #54: Large ribosomal subunit protein uL4
+Macromolecule #55: Large ribosomal subunit protein uL6
+Macromolecule #56: Large ribosomal subunit protein eL30
+Macromolecule #57: Large ribosomal subunit protein eL18
+Macromolecule #58: Large ribosomal subunit protein eL15
+Macromolecule #59: Large ribosomal subunit protein uL22
+Macromolecule #60: Large ribosomal subunit protein eL34
+Macromolecule #61: Large ribosomal subunit protein uL16
+Macromolecule #62: Large ribosomal subunit protein eL40
+Macromolecule #63: Large ribosomal subunit protein eL33
+Macromolecule #64: Large ribosomal subunit protein uL14
+Macromolecule #65: Large ribosomal subunit protein eL20
+Macromolecule #66: C2H2-type domain-containing protein
+Macromolecule #67: Large ribosomal subunit protein uL1
+Macromolecule #68: MAGNESIUM ION
+Macromolecule #69: ZINC 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: 7.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 40.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Pyrococcus abyssi GE5 (archaea)
Authors
France, 1 items
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Processing
FIELD EMISSION GUN


