+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-9236 | |||||||||
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Title | Rabbit 80S ribosome with a Z-site tRNA (unrotated state) | |||||||||
Map data | Postprocessed map | |||||||||
Sample |
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Biological species | Oryctolagus cuniculus (rabbit) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.2 Å | |||||||||
Authors | Brown A / Baird MR / Yip MCJ / Murray J / Shao S | |||||||||
Citation | Journal: Elife / Year: 2018 Title: Structures of translationally inactive mammalian ribosomes. Authors: Alan Brown / Matthew R Baird / Matthew Cj Yip / Jason Murray / Sichen Shao / Abstract: The cellular levels and activities of ribosomes directly regulate gene expression during numerous physiological processes. The mechanisms that globally repress translation are incompletely understood. ...The cellular levels and activities of ribosomes directly regulate gene expression during numerous physiological processes. The mechanisms that globally repress translation are incompletely understood. Here, we use electron cryomicroscopy to analyze inactive ribosomes isolated from mammalian reticulocytes, the penultimate stage of red blood cell differentiation. We identify two types of ribosomes that are translationally repressed by protein interactions. The first comprises ribosomes sequestered with elongation factor 2 (eEF2) by SERPINE mRNA binding protein 1 (SERBP1) occupying the ribosomal mRNA entrance channel. The second type are translationally repressed by a novel ribosome-binding protein, interferon-related developmental regulator 2 (IFRD2), which spans the P and E sites and inserts a C-terminal helix into the mRNA exit channel to preclude translation. IFRD2 binds ribosomes with a tRNA occupying a noncanonical binding site, the 'Z site', on the ribosome. These structures provide functional insights into how ribosomal interactions may suppress translation to regulate gene expression. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_9236.map.gz | 11.3 MB | EMDB map data format | |
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Header (meta data) | emd-9236-v30.xml emd-9236.xml | 15.7 KB 15.7 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_9236_fsc.xml | 14.2 KB | Display | FSC data file |
Images | emd_9236.png | 168 KB | ||
Others | emd_9236_additional.map.gz emd_9236_additional_1.map.gz emd_9236_half_map_1.map.gz emd_9236_half_map_2.map.gz | 217.9 MB 217.9 MB 215.7 MB 215.7 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-9236 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-9236 | HTTPS FTP |
-Validation report
Summary document | emd_9236_validation.pdf.gz | 78.4 KB | Display | EMDB validaton report |
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Full document | emd_9236_full_validation.pdf.gz | 77.5 KB | Display | |
Data in XML | emd_9236_validation.xml.gz | 494 B | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-9236 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-9236 | HTTPS FTP |
-Related structure data
Related structure data | 9234C 9235C 9237C 9239C 9240C 9241C 9242C 6mtbC 6mtcC 6mtdC 6mteC C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_9236.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Postprocessed map | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.34 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Additional map: Pre-postprocessed map
File | emd_9236_additional.map | ||||||||||||
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Annotation | Pre-postprocessed map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: Pre-postprocessed map
File | emd_9236_additional_1.map | ||||||||||||
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Annotation | Pre-postprocessed map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map 2
File | emd_9236_half_map_1.map | ||||||||||||
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Annotation | Half map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map 1
File | emd_9236_half_map_2.map | ||||||||||||
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Annotation | Half map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Rabbit 80S ribosome with a Z-site tRNA (unrotated state)
Entire | Name: Rabbit 80S ribosome with a Z-site tRNA (unrotated state) |
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Components |
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-Supramolecule #1: Rabbit 80S ribosome with a Z-site tRNA (unrotated state)
Supramolecule | Name: Rabbit 80S ribosome with a Z-site tRNA (unrotated state) type: complex / ID: 1 / Parent: 0 |
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Source (natural) | Organism: Oryctolagus cuniculus (rabbit) / Location in cell: cytoplasm |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK II |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON II (4k x 4k) / Detector mode: INTEGRATING / Digitization - Frames/image: 1-17 / Average exposure time: 1.1 sec. / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Calibrated magnification: 104478 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |