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- EMDB-11325: SARS-CoV-2 Nsp1 bound to a human 43S preinitiation ribosome compl... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-11325 | ||||||||||||
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Title | SARS-CoV-2 Nsp1 bound to a human 43S preinitiation ribosome complex - state 1 | ||||||||||||
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![]() | SARS-CoV-2 Nsp1 bound to a human 43S preinitiation ribosome complex - state 1
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Function / homology | ![]() cap-dependent translational initiation / viral translational termination-reinitiation / eukaryotic translation initiation factor 3 complex, eIF3e / eukaryotic translation initiation factor 3 complex, eIF3m / translation reinitiation / positive regulation of mRNA binding / mRNA cap binding / IRES-dependent viral translational initiation / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() | ||||||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() | ||||||||||||
Method | ![]() ![]() | ||||||||||||
![]() | Thoms M / Buschauer R / Ameismeier M / Denk T / Kratzat H / Mackens-Kiani T / Cheng J / Berninghausen O / Becker T / Beckmann R | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis for translational shutdown and immune evasion by the Nsp1 protein of SARS-CoV-2. Authors: Matthias Thoms / Robert Buschauer / Michael Ameismeier / Lennart Koepke / Timo Denk / Maximilian Hirschenberger / Hanna Kratzat / Manuel Hayn / Timur Mackens-Kiani / Jingdong Cheng / Jan H ...Authors: Matthias Thoms / Robert Buschauer / Michael Ameismeier / Lennart Koepke / Timo Denk / Maximilian Hirschenberger / Hanna Kratzat / Manuel Hayn / Timur Mackens-Kiani / Jingdong Cheng / Jan H Straub / Christina M Stürzel / Thomas Fröhlich / Otto Berninghausen / Thomas Becker / Frank Kirchhoff / Konstantin M J Sparrer / Roland Beckmann / ![]() Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the current coronavirus disease 2019 (COVID-19) pandemic. A major virulence factor of SARS-CoVs is the ...Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the current coronavirus disease 2019 (COVID-19) pandemic. A major virulence factor of SARS-CoVs is the nonstructural protein 1 (Nsp1), which suppresses host gene expression by ribosome association. Here, we show that Nsp1 from SARS-CoV-2 binds to the 40 ribosomal subunit, resulting in shutdown of messenger RNA (mRNA) translation both in vitro and in cells. Structural analysis by cryo-electron microscopy of in vitro-reconstituted Nsp1-40 and various native Nsp1-40 and -80 complexes revealed that the Nsp1 C terminus binds to and obstructs the mRNA entry tunnel. Thereby, Nsp1 effectively blocks retinoic acid-inducible gene I-dependent innate immune responses that would otherwise facilitate clearance of the infection. Thus, the structural characterization of the inhibitory mechanism of Nsp1 may aid structure-based drug design against SARS-CoV-2. | ||||||||||||
Validation Report | ![]() ![]() ![]() ![]() | ||||||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
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Download
FSC (resolution estimation) |
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Header (meta data in XML format) |
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Images |
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Archive directory |
-Related structure data
Related structure data | ![]() 6zonCM ![]() 6zlwC ![]() 6zm7C ![]() 6zmeC ![]() 6zmiC ![]() 6zmoC ![]() 6zmtC ![]() 6zn5C ![]() 6zp4C C: citing same article ( M: atomic model generated by this map |
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Similar-shape strucutres |
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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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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.059 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
+Entire SARS-CoV-2 Nsp1 bound to a human 43S preinitiation ribosome compl...
+Component #1: protein, SARS-CoV-2 Nsp1 bound to a human 43S preinitiation ribos...
+Component #2: protein, Human 43S preinitiation ribosome complex
+Component #3: protein, SARS-CoV-2 Nsp1
+Component #4: protein, 40S ribosomal protein SA
+Component #5: protein, 40S ribosomal protein S3a
+Component #6: protein, 40S ribosomal protein S2
+Component #7: protein, 40S ribosomal protein S26
+Component #8: protein, 40S ribosomal protein S4, X isoform
+Component #9: protein, 60S ribosomal protein L41
+Component #10: protein, 40S ribosomal protein S6
+Component #11: protein, 40S ribosomal protein S7
+Component #12: protein, 40S ribosomal protein S8
+Component #13: protein, 40S ribosomal protein S9
+Component #14: protein, 40S ribosomal protein S11
+Component #15: protein, 40S ribosomal protein S13
+Component #16: protein, 40S ribosomal protein S14
+Component #17: protein, 40S ribosomal protein S21
+Component #18: protein, 40S ribosomal protein S15a
+Component #19: protein, 40S ribosomal protein S23
+Component #20: protein, 40S ribosomal protein S24
+Component #21: protein, 40S ribosomal protein S27
+Component #22: protein, 40S ribosomal protein S30
+Component #23: nucleic-acid, 18S ribosomal RNA
+Component #24: protein, 40S ribosomal protein S17
+Component #25: protein, 40S ribosomal protein S16
+Component #26: protein, 40S ribosomal protein S3
+Component #27: protein, 40S ribosomal protein S5
+Component #28: protein, 40S ribosomal protein S10
+Component #29: protein, 40S ribosomal protein S12
+Component #30: protein, 40S ribosomal protein S15
+Component #31: protein, 40S ribosomal protein S18
+Component #32: protein, 40S ribosomal protein S19
+Component #33: protein, 40S ribosomal protein S20
+Component #34: protein, 40S ribosomal protein S25
+Component #35: protein, 40S ribosomal protein S28
+Component #36: protein, 40S ribosomal protein S29
+Component #37: protein, Ubiquitin-40S ribosomal protein S27a
+Component #38: protein, Receptor of activated protein C kinase 1
+Component #39: protein, Eukaryotic translation initiation factor 3 subunit I
+Component #40: protein, Eukaryotic translation initiation factor 3 subunit B
+Component #41: protein, Eukaryotic translation initiation factor 3 subunit A,Euk...
+Component #42: protein, Eukaryotic translation initiation factor 3 subunit C
+Component #43: protein, Eukaryotic translation initiation factor 3 subunit E
+Component #44: protein, Eukaryotic translation initiation factor 3 subunit F
+Component #45: protein, Eukaryotic translation initiation factor 3 subunit H
+Component #46: protein, Eukaryotic translation initiation factor 3 subunit K
+Component #47: protein, Eukaryotic translation initiation factor 3 subunit L
+Component #48: protein, Eukaryotic translation initiation factor 3 subunit M
+Component #49: protein, Eukaryotic translation initiation factor 3 subunit D
+Component #50: protein, Unknown factor
+Component #51: protein, Host translation inhibitor Nsp1
+Component #52: ligand, ZINC ION
-Experimental details
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Sample preparation
Specimen | Specimen state: Particle / Method: ![]() |
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Sample solution | pH: 7.5 |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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![]() | Microscope: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN![]() |
Lens | Imaging mode: BRIGHT FIELD![]() |
Specimen Holder | Model: OTHER |
Camera | Detector: GATAN K2 SUMMIT (4k x 4k) |
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Image processing
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3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF |
FSC plot (resolution estimation)![]() | ![]() |
-Atomic model buiding
Output model |
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