7CN8

Cryo-EM structure of PCoV_GX spike glycoprotein

Summary for 7CN8

• Entry DOI: 10.2210/pdb7cn8/pdb
• EMDB information: 30418
• Descriptor: Glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• Functional Keywords: spike, viral protein
• Biological source: Pangolin coronavirus
• Total number of polymer chains: 3
• Total formula weight: 451324.95

Authors

Wang, X.,Yu, J.,Zhang, S.,Qiao, S.,Zeng, J.,Tian, L. (deposition date: 2020-07-30, release date: 2021-03-03, Last modification date: 2024-11-06)

Primary citation

Zhang, S.,Qiao, S.,Yu, J.,Zeng, J.,Shan, S.,Tian, L.,Lan, J.,Zhang, L.,Wang, X.
Bat and pangolin coronavirus spike glycoprotein structures provide insights into SARS-CoV-2 evolution.
Nat Commun, 12:1607-1607, 2021

PubMed Abstract: In recognizing the host cellular receptor and mediating fusion of virus and cell membranes, the spike (S) glycoprotein of coronaviruses is the most critical viral protein for cross-species transmission and infection. Here we determined the cryo-EM structures of the spikes from bat (RaTG13) and pangolin (PCoV_GX) coronaviruses, which are closely related to SARS-CoV-2. All three receptor-binding domains (RBDs) of these two spike trimers are in the "down" conformation, indicating they are more prone to adopt the receptor-binding inactive state. However, we found that the PCoV_GX, but not the RaTG13, spike is comparable to the SARS-CoV-2 spike in binding the human ACE2 receptor and supporting pseudovirus cell entry. We further identified critical residues in the RBD underlying different activities of the RaTG13 and PCoV_GX/SARS-CoV-2 spikes. These results collectively indicate that tight RBD-ACE2 binding and efficient RBD conformational sampling are required for the evolution of SARS-CoV-2 to gain highly efficient infection.

PubMed: 33707453
DOI: 10.1038/s41467-021-21767-3

Experimental method

ELECTRON MICROSCOPY (2.5 Å)