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Yorodumi- EMDB-41063: MERS-CoV Nsp1 protein binds the human 40S ribosome - Consensus Re... -
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Open data
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Basic information
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| Title | MERS-CoV Nsp1 protein binds the human 40S ribosome - Consensus Reconstruction | |||||||||
Map data | Consensus Refinement Reconstruction | |||||||||
Sample |
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Keywords | MERS-CoV Nsp1 / translation inhibition / 40S ribosome / betacoronaviruses / RIBOSOME | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.6 Å | |||||||||
Authors | Devarkar SC / Xiong Y | |||||||||
| Funding support | United States, 1 items
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Citation | Journal: Cell Rep / Year: 2023Title: Structural basis for translation inhibition by MERS-CoV Nsp1 reveals a conserved mechanism for betacoronaviruses. Authors: Swapnil C Devarkar / Michael Vetick / Shravani Balaji / Ivan B Lomakin / Luojia Yang / Danni Jin / Wendy V Gilbert / Sidi Chen / Yong Xiong / ![]() Abstract: All betacoronaviruses (β-CoVs) encode non-structural protein 1 (Nsp1), an essential pathogenicity factor that potently restricts host gene expression. Among the β-CoV family, MERS-CoV is the most ...All betacoronaviruses (β-CoVs) encode non-structural protein 1 (Nsp1), an essential pathogenicity factor that potently restricts host gene expression. Among the β-CoV family, MERS-CoV is the most distantly related member to SARS-CoV-2, and the mechanism for host translation inhibition by MERS-CoV Nsp1 remains controversial. Herein, we show that MERS-CoV Nsp1 directly interacts with the 40S ribosomal subunit. Using cryogenic electron microscopy (cryo-EM), we report a 2.6-Å structure of the MERS-CoV Nsp1 bound to the human 40S ribosomal subunit. The extensive interactions between C-terminal domain of MERS-CoV Nsp1 and the mRNA entry channel of the 40S ribosomal subunit are critical for its translation inhibition function. This mechanism of MERS-CoV Nsp1 is strikingly similar to SARS-CoV and SARS-CoV-2 Nsp1, despite modest sequence conservation. Our results reveal that the mechanism of host translation inhibition is conserved across β-CoVs and highlight a potential therapeutic target for the development of antivirals that broadly restrict β-CoVs. | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_41063.map.gz | 105.9 MB | EMDB map data format | |
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| Header (meta data) | emd-41063-v30.xml emd-41063.xml | 17.3 KB 17.3 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_41063_fsc.xml | 12.4 KB | Display | FSC data file |
| Images | emd_41063.png | 46.1 KB | ||
| Filedesc metadata | emd-41063.cif.gz | 4 KB | ||
| Others | emd_41063_half_map_1.map.gz emd_41063_half_map_2.map.gz | 194.1 MB 194.1 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-41063 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-41063 | HTTPS FTP |
-Validation report
| Summary document | emd_41063_validation.pdf.gz | 973.4 KB | Display | EMDB validaton report |
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| Full document | emd_41063_full_validation.pdf.gz | 972.9 KB | Display | |
| Data in XML | emd_41063_validation.xml.gz | 21.6 KB | Display | |
| Data in CIF | emd_41063_validation.cif.gz | 28.1 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-41063 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-41063 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_41063.map.gz / Format: CCP4 / Size: 209.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Consensus Refinement Reconstruction | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.07 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: Halfmap B consensus
| File | emd_41063_half_map_1.map | ||||||||||||
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| Annotation | Halfmap B_consensus | ||||||||||||
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| Density Histograms |
-Half map: Halfmap A consensus
| File | emd_41063_half_map_2.map | ||||||||||||
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| Annotation | Halfmap A_consensus | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : MERS-CoV Nsp1 bound to human 40S ribosomal subunit
| Entire | Name: MERS-CoV Nsp1 bound to human 40S ribosomal subunit |
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| Components |
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-Supramolecule #1: MERS-CoV Nsp1 bound to human 40S ribosomal subunit
| Supramolecule | Name: MERS-CoV Nsp1 bound to human 40S ribosomal subunit / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#36 |
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| Source (natural) | Organism: Homo sapiens (human) |
-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 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 81000 |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
Homo sapiens (human)
Authors
United States, 1 items
Citation



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Processing
FIELD EMISSION GUN


