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Yorodumi- EMDB-54789: Cryo-EM structure of the Arabidopsis thaliana 40S ribosomal subunit -
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Open data
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Basic information
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| Title | Cryo-EM structure of the Arabidopsis thaliana 40S ribosomal subunit | |||||||||
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Keywords | Arabidopsis / Ribosome / CryoEM | |||||||||
| Function / homology | Function and homology informationtrichome morphogenesis / cytokinesis by cell plate formation / leaf morphogenesis / chloroplast organization / plant-type cell wall / plasmodesma / plant-type vacuole / plastid / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) ...trichome morphogenesis / cytokinesis by cell plate formation / leaf morphogenesis / chloroplast organization / plant-type cell wall / plasmodesma / plant-type vacuole / plastid / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / cytosolic ribosome / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / small-subunit processome / chloroplast / rRNA processing / ribosomal small subunit assembly / ribosomal small subunit biogenesis / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / cytoplasmic translation / defense response to bacterium / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / mRNA binding / nucleolus / endoplasmic reticulum / mitochondrion / RNA binding / zinc ion binding / nucleus / plasma membrane / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
Authors | Karki S / Lu X / Paatero AO / Ruonala R / Tranter D / Guryanov S / Rehan S / Hellmann E / Haakonsson A / Butcher SJ ...Karki S / Lu X / Paatero AO / Ruonala R / Tranter D / Guryanov S / Rehan S / Hellmann E / Haakonsson A / Butcher SJ / Huiskonen JT / Kajander T / Helariutta Y / Paavilainen VO | |||||||||
| Funding support | United States, Finland, 2 items
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Citation | Journal: Structure / Year: 2026Title: Cryo-EM structure of the Arabidopsisthaliana ribosome in translating and non-translating states. Authors: Sudeep Karki / Xun Lu / Anja O Paatero / Raili Ruonala / Dale Tranter / Sergey Guryanov / Shahid Rehan / Eva Hellmann / Anders Haakonsson / Sarah J Butcher / Juha T Huiskonen / Tommi ...Authors: Sudeep Karki / Xun Lu / Anja O Paatero / Raili Ruonala / Dale Tranter / Sergey Guryanov / Shahid Rehan / Eva Hellmann / Anders Haakonsson / Sarah J Butcher / Juha T Huiskonen / Tommi Kajander / Yrjö Helariutta / Ville O Paavilainen / ![]() Abstract: Translational control of mRNA expression underpins much of post-transcriptional gene expression driving developmental processes in eukaryotes. How ribosomal mRNA translation is executed in plants may ...Translational control of mRNA expression underpins much of post-transcriptional gene expression driving developmental processes in eukaryotes. How ribosomal mRNA translation is executed in plants may be especially important for adapting to an ever-changing environment. Arabidopsis thaliana is the main genetic model organism in plant science, yet structural insights into developmental processes where ribosomal gene expression plays important roles currently remain lacking. Here, we present cryoelectron microscopy (cryo-EM) structures of the Arabidopsis cytosolic ribosome in both translating and non-translating states, which together provide new structural details into how translation of cytosolic mRNAs is coordinated. Our structures reveal detailed information on the interactions of tRNAs, mRNA, and the nascent polypeptide with subunits of the actively translating 80S ribosome and the role of ribosomal RNA methylation in stabilizing ribosomal subunits. The structures provide a foundation for interpreting the functional effects of many mutations of ribosomal proteins affecting phenotypic effects for plant tissue development. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_54789.map.gz | 173.3 MB | EMDB map data format | |
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| Header (meta data) | emd-54789-v30.xml emd-54789.xml | 40.7 KB 40.7 KB | Display Display | EMDB header |
| Images | emd_54789.png | 71.2 KB | ||
| Filedesc metadata | emd-54789.cif.gz | 10 KB | ||
| Others | emd_54789_half_map_1.map.gz emd_54789_half_map_2.map.gz | 323 MB 323 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-54789 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-54789 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9sdpMC ![]() 9scuC ![]() 9sdqC 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_54789.map.gz / Format: CCP4 / Size: 347.6 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: 0.84 Å | ||||||||||||||||||||||||||||||||||||
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_54789_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_54789_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
+Entire : 60S LSU Arabidopsis (root) ribosome complex
+Supramolecule #1: 60S LSU Arabidopsis (root) ribosome complex
+Macromolecule #1: 18S RNA
+Macromolecule #2: Small ribosomal subunit protein uS2y
+Macromolecule #3: Small ribosomal subunit protein eS1z
+Macromolecule #4: Small ribosomal subunit protein uS5w
+Macromolecule #5: Small ribosomal subunit protein eS4z
+Macromolecule #6: Small ribosomal subunit protein eS6y
+Macromolecule #7: Small ribosomal subunit protein eS7z
+Macromolecule #8: Small ribosomal subunit protein eS8z
+Macromolecule #9: Small ribosomal subunit protein uS4y
+Macromolecule #10: Small ribosomal subunit protein uS17z
+Macromolecule #11: Small ribosomal subunit protein uS15y
+Macromolecule #12: Small ribosomal subunit protein uS11x
+Macromolecule #13: Small ribosomal subunit protein eS21z
+Macromolecule #14: Small ribosomal subunit protein uS8z/uS8w
+Macromolecule #15: Small ribosomal subunit protein uS12y
+Macromolecule #16: Small ribosomal subunit protein eS24z
+Macromolecule #17: Small ribosomal subunit protein eS26x
+Macromolecule #18: Small ribosomal subunit protein eS27y
+Macromolecule #19: Small ribosomal subunit protein eS30z/eS30y/eS30x
+Macromolecule #20: Small ribosomal subunit protein eS32 eS32z/eS32y/eS32x/eS32w/eS32v
+Macromolecule #21: POTASSIUM ION
+Macromolecule #22: MAGNESIUM ION
+Macromolecule #23: ZINC ION
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | tissue |
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Sample preparation
| Buffer | pH: 7.4 Details: 50 mM Hepes, pH 7.4, 5 mM MgAc, 100 mM KAc, pH 7.5, 1 mM DTT, Complete protease inhibitor |
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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 (6k x 4k) / Average electron dose: 24.512 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: OTHER / Imaging mode: OTHER / Cs: 2.7 mm / Nominal defocus max: 1.2 µm / Nominal defocus min: 0.6 µm / Nominal magnification: 105000 |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Authors
United States,
Finland, 2 items
Citation









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Processing
FIELD EMISSION GUN
