5X59

Prefusion structure of MERS-CoV spike glycoprotein, three-fold symmetry

Summary for 5X59

• Entry DOI: 10.2210/pdb5x59/pdb
• EMDB information: 6704
• Descriptor: S protein, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• Functional Keywords: mers-cov, spike glycoprotein, prefusion, single particle, viral protein
• Biological source: Middle East respiratory syndrome coronavirus
• Total number of polymer chains: 3
• Total formula weight: 444204.85

Authors

Yuan, Y.,Cao, D.,Zhang, Y.,Ma, J.,Qi, J.,Wang, Q.,Lu, G.,Wu, Y.,Yan, J.,Shi, Y.,Zhang, X.,Gao, G.F. (deposition date: 2017-02-15, release date: 2017-05-03, Last modification date: 2024-10-30)

Primary citation

Yuan, Y.,Cao, D.,Zhang, Y.,Ma, J.,Qi, J.,Wang, Q.,Lu, G.,Wu, Y.,Yan, J.,Shi, Y.,Zhang, X.,Gao, G.F.
Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains
Nat Commun, 8:15092-15092, 2017

PubMed 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 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.

PubMed: 28393837
DOI: 10.1038/ncomms15092

Experimental method

ELECTRON MICROSCOPY (3.7 Å)