7CN4

Cryo-EM structure of bat RaTG13 spike glycoprotein

7CN4 の概要

• エントリーDOI: 10.2210/pdb7cn4/pdb
• EMDBエントリー: 30416
• 分子名称: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: spike, viral protein
• 由来する生物種: Bat coronavirus RaTG13
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 433321.25

構造登録者

Wang, X.,Zhang, S.,Qiao, S.,Yu, J.,Zeng, J.,Tian, L. (登録日: 2020-07-30, 公開日: 2021-03-03, 最終更新日: 2024-10-23)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (2.93 Å)