|Entry||Database: EMDB / ID: EMD-6681|
|Title||SARS-CoV Spike Conformation 3|
|Map data||SARS-CoV Spike conformation 3|
|Biological species||SARS coronavirus|
|Method||single particle reconstruction / cryo EM / Resolution: 5.7 Å|
|Authors||Gui M / Song W / Xiang Y / Wang X|
|Citation||Journal: Cell Res / Year: 2017|
Title: Cryo-electron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding.
Authors: Miao Gui / Wenfei Song / Haixia Zhou / Jingwei Xu / Silian Chen / Ye Xiang / Xinquan Wang /
Abstract: The global outbreak of SARS in 2002-2003 was caused by the infection of a new human coronavirus SARS-CoV. The infection of SARS-CoV is mediated mainly through the viral surface glycoproteins, which ...The global outbreak of SARS in 2002-2003 was caused by the infection of a new human coronavirus SARS-CoV. The infection of SARS-CoV is mediated mainly through the viral surface glycoproteins, which consist of S1 and S2 subunits and form trimer spikes on the envelope of the virions. Here we report the ectodomain structures of the SARS-CoV surface spike trimer in different conformational states determined by single-particle cryo-electron microscopy. The conformation 1 determined at 4.3 Å resolution is three-fold symmetric and has all the three receptor-binding C-terminal domain 1 (CTD1s) of the S1 subunits in "down" positions. The binding of the "down" CTD1s to the SARS-CoV receptor ACE2 is not possible due to steric clashes, suggesting that the conformation 1 represents a receptor-binding inactive state. Conformations 2-4 determined at 7.3, 5.7 and 6.8 Å resolutions are all asymmetric, in which one RBD rotates away from the "down" position by different angles to an "up" position. The "up" CTD1 exposes the receptor-binding site for ACE2 engagement, suggesting that the conformations 2-4 represent a receptor-binding active state. This conformational change is also required for the binding of SARS-CoV neutralizing antibodies targeting the CTD1. This phenomenon could be extended to other betacoronaviruses utilizing CTD1 of the S1 subunit for receptor binding, which provides new insights into the intermediate states of coronavirus pre-fusion spike trimer during infection.
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_6681.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Annotation||SARS-CoV Spike conformation 3|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.32 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire : SARS-CoV spike glycoprotein
|Entire||Name: SARS-CoV spike glycoprotein|
-Supramolecule #1: SARS-CoV spike glycoprotein
|Supramolecule||Name: SARS-CoV spike glycoprotein / type: complex / ID: 1 / Parent: 0|
|Source (natural)||Organism: SARS coronavirus|
|Recombinant expression||Organism: Spodoptera frugiperda (fall armyworm) / Recombinant plasmid: pFastBac-Dual|
|Molecular weight||Theoretical: 400 KDa|
|Processing||single particle reconstruction|
|Vitrification||Cryogen name: ETHANE|
|Microscope||FEI TITAN KRIOS|
|Electron beam||Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN|
|Electron optics||Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy|
|Image recording||Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average exposure time: 8.0 sec. / Average electron dose: 4.7 e/Å2|
Model: Titan Krios / Image courtesy: FEI Company
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