|Entry||Database: EMDB / ID: 6707|
|Title||Prefusion structure of MERS-CoV spike glycoprotein, conformation 2|
|Sample||MERS-CoV spike trimer|
|Function/homology||host cell endoplasmic reticulum-Golgi intermediate compartment membrane / Spike receptor binding domain / Spike receptor binding domain superfamily / Coronovirus spike glycoprotein, heptad repeat 2 domain / Coronavirus S2 glycoprotein / Coronavirus S2 glycoprotein / Spike receptor binding domain / membrane fusion / receptor-mediated virion attachment to host cell / fusion of virus membrane with host plasma membrane ...host cell endoplasmic reticulum-Golgi intermediate compartment membrane / Spike receptor binding domain / Spike receptor binding domain superfamily / Coronovirus spike glycoprotein, heptad repeat 2 domain / Coronavirus S2 glycoprotein / Coronavirus S2 glycoprotein / Spike receptor binding domain / membrane fusion / receptor-mediated virion attachment to host cell / fusion of virus membrane with host plasma membrane / pathogenesis / viral envelope / virion membrane / integral component of membrane / Spike glycoprotein / S protein|
Function and homology information
|Source||Middle East respiratory syndrome coronavirus / / virus|
|Method||Cryo EM / single particle reconstruction / 4.2 Å resolution|
|Authors||Yuan Y / Cao D|
|Citation||Journal: Nat Commun / Year: 2017|
Title: Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains.
Authors: Yuan Yuan / Duanfang Cao / Yanfang Zhang / Jun Ma / Jianxun Qi / Qihui Wang / Guangwen Lu / Ying Wu / Jinghua Yan / Yi Shi / Xinzheng Zhang / George F Gao
Abstract: The envelope spike (S) proteins of MERS-CoV and SARS-CoV determine the virus host tropism and entry into host cells, and constitute a promising target for the development of prophylactics and ...The envelope spike (S) proteins of MERS-CoV and SARS-CoV determine the virus host tropism and entry into host cells, and constitute a promising target for the development of prophylactics and therapeutics. Here, we present high-resolution structures of the trimeric MERS-CoV and SARS-CoV S proteins in its pre-fusion conformation by single particle cryo-electron microscopy. The overall structures resemble that from other coronaviruses including HKU1, MHV and NL63 reported recently, with the exception of the receptor binding domain (RBD). We captured two states of the RBD with receptor binding region either buried (lying state) or exposed (standing state), demonstrating an inherently flexible RBD readily recognized by the receptor. Further sequence conservation analysis of six human-infecting coronaviruses revealed that the fusion peptide, HR1 region and the central helix are potential targets for eliciting broadly neutralizing antibodies.
|Validation Report||PDB-ID: 5x5f|
SummaryFull reportAbout validation report
|Date||Deposition: Feb 15, 2017 / Header (metadata) release: May 3, 2017 / Map release: May 3, 2017 / Last update: May 24, 2017|
Downloads & links
|File||emd_6707.map.gz (map file in CCP4 format, 32001 KB)|
|Projections & slices|
Images are generated by Spider package.
|Voxel size||X=Y=Z: 1.3 Å|
CCP4 map header:
-Entire MERS-CoV spike trimer
|Entire||Name: MERS-CoV spike trimer / Number of components: 2|
-Component #1: protein, MERS-CoV spike trimer
|Protein||Name: MERS-CoV spike trimer / Recombinant expression: No|
|Source||Species: Middle East respiratory syndrome coronavirus / / virus|
|Source (engineered)||Expression System: Spodoptera frugiperda / Fall armyworm / arthropod|
-Component #2: protein, S protein
|Protein||Name: S protein / Recombinant expression: No|
|Mass||Theoretical: 145.856203 kDa|
|Source (engineered)||Expression System: Middle East respiratory syndrome coronavirus / / virus|
|Specimen||Specimen state: particle / Method: Cryo EM|
|Sample solution||pH: 7.5|
|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: 8 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: GATAN K2 (4k x 4k)|
|Processing||Method: single particle reconstruction / Number of projections: 60000|
|3D reconstruction||Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF|
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