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- EMDB-6681: SARS-CoV Spike Conformation 3 -

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Basic information

Database: EMDB / ID: EMD-6681
TitleSARS-CoV Spike Conformation 3
Map dataSARS-CoV Spike conformation 3
  • Complex: SARS-CoV spike glycoprotein
Biological speciesSARS coronavirus
Methodsingle particle reconstruction / cryo EM / Resolution: 5.7 Å
AuthorsGui M / Song W / Xiang Y / Wang X
CitationJournal: 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.
DepositionDec 1, 2016-
Header (metadata) releaseJan 11, 2017-
Map releaseJan 11, 2017-
UpdateDec 13, 2017-
Current statusDec 13, 2017Processing site: PDBj / Status: Released

Structure visualization

  • Surface view with section colored by density value
  • Surface level: 0.02
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.02
  • Imaged by UCSF Chimera
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Structure viewerEM map:
Supplemental images

Downloads & links


FileDownload / File: emd_6681.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationSARS-CoV Spike conformation 3
Projections & slices

Image control

AxesZ (Sec.)Y (Row.)X (Col.)
1.32 Å/pix.
x 288 pix.
= 380.16 Å
1.32 Å/pix.
x 288 pix.
= 380.16 Å
1.32 Å/pix.
x 288 pix.
= 380.16 Å



Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.32 Å
Contour LevelBy AUTHOR: 0.02 / Movie #1: 0.02
Minimum - Maximum-0.0329936 - 0.10422362
Average (Standard dev.)0.00025296884 (±0.002996506)
SymmetrySpace group: 1


Map geometry
Axis orderXYZ
CellA=B=C: 380.16 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.321.321.32
M x/y/z288288288
origin x/y/z0.0000.0000.000
length x/y/z380.160380.160380.160
MAP C/R/S123
start NC/NR/NS000
D min/max/mean-0.0330.1040.000

Supplemental data

Sample components

Entire : SARS-CoV spike glycoprotein

EntireName: SARS-CoV spike glycoprotein
  • Complex: SARS-CoV spike glycoprotein

Supramolecule #1: SARS-CoV spike glycoprotein

SupramoleculeName: SARS-CoV spike glycoprotein / type: complex / ID: 1 / Parent: 0
Source (natural)Organism: SARS coronavirus
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm) / Recombinant plasmid: pFastBac-Dual
Molecular weightTheoretical: 400 KDa

Experimental details

Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

Sample preparation

BufferpH: 7.2
VitrificationCryogen name: ETHANE

Electron microscopy

Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average exposure time: 8.0 sec. / Average electron dose: 4.7 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

Image processing

CTF correctionSoftware - Name: CTFFIND (ver. 4.0)
Initial angle assignmentType: RANDOM ASSIGNMENT / Software - Name: RELION (ver. 1.4)
Final angle assignmentType: PROJECTION MATCHING / Software - Name: RELION (ver. 1.4)
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 5.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 1.4) / Number images used: 39350
FSC plot (resolution estimation)

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