|Entry||Database: EMDB / ID: EMD-9584|
|Title||Trypsin-cleaved SARS-CoV spike glycoprotein and ACE2 complex, ACE2-free conformation with one RBD in up position|
|Sample||Trypsin-cleaved SARS-CoV spike glycoprotein|
|Biological species||SARS coronavirus|
|Method||single particle reconstruction / cryo EM / Resolution: 9 Å|
|Authors||Gui M / Song W|
|Citation||Journal: PLoS Pathog / Year: 2018|
Title: Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2.
Authors: Wenfei Song / Miao Gui / Xinquan Wang / Ye Xiang /
Abstract: The trimeric SARS coronavirus (SARS-CoV) surface spike (S) glycoprotein consisting of three S1-S2 heterodimers binds the cellular receptor angiotensin-converting enzyme 2 (ACE2) and mediates fusion ...The trimeric SARS coronavirus (SARS-CoV) surface spike (S) glycoprotein consisting of three S1-S2 heterodimers binds the cellular receptor angiotensin-converting enzyme 2 (ACE2) and mediates fusion of the viral and cellular membranes through a pre- to postfusion conformation transition. Here, we report the structure of the SARS-CoV S glycoprotein in complex with its host cell receptor ACE2 revealed by cryo-electron microscopy (cryo-EM). The complex structure shows that only one receptor-binding domain of the trimeric S glycoprotein binds ACE2 and adopts a protruding "up" conformation. In addition, we studied the structures of the SARS-CoV S glycoprotein and its complexes with ACE2 in different in vitro conditions, which may mimic different conformational states of the S glycoprotein during virus entry. Disassociation of the S1-ACE2 complex from some of the prefusion spikes was observed and characterized. We also characterized the rosette-like structures of the clustered SARS-CoV S2 trimers in the postfusion state observed on electron micrographs. Structural comparisons suggested that the SARS-CoV S glycoprotein retains a prefusion architecture after trypsin cleavage into the S1 and S2 subunits and acidic pH treatment. However, binding to the receptor opens up the receptor-binding domain of S1, which could promote the release of the S1-ACE2 complex and S1 monomers from the prefusion spike and trigger the pre- to postfusion conformational transition.
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_9584.map.gz / Format: CCP4 / Size: 7.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 2.54 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire Trypsin-cleaved SARS-CoV spike glycoprotein
|Entire||Name: Trypsin-cleaved SARS-CoV spike glycoprotein / Number of components: 1|
-Component #1: protein, Trypsin-cleaved SARS-CoV spike glycoprotein
|Protein||Name: Trypsin-cleaved SARS-CoV spike glycoprotein / Recombinant expression: No|
|Mass||Theoretical: 400 kDa|
|Source||Species: SARS coronavirus|
|Source (engineered)||Expression System: Spodoptera frugiperda (fall armyworm)|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||pH: 7.2|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 50 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
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