7C8D

Cryo-EM structure of cat ACE2 and SARS-CoV-2 RBD

Summary for 7C8D

• Entry DOI: 10.2210/pdb7c8d/pdb
• EMDB information: 30305
• Descriptor: Angiotensin-converting enzyme 2, Spike protein S1, ZINC ION (3 entities in total)
• Functional Keywords: ace2, sars-cov-2, cryo-em, complex, protein binding, hydrolase-viral protein complex, hydrolase/viral protein
• Biological source: Felis catus (Cat); More
• Total number of polymer chains: 2
• Total formula weight: 107071.86

Authors

Gao, G.F.,Wang, Q.H.,Wu, L.l. (deposition date: 2020-05-29, release date: 2020-09-02, Last modification date: 2024-11-20)

Primary citation

Wu, L.,Chen, Q.,Liu, K.,Wang, J.,Han, P.,Zhang, Y.,Hu, Y.,Meng, Y.,Pan, X.,Qiao, C.,Tian, S.,Du, P.,Song, H.,Shi, W.,Qi, J.,Wang, H.W.,Yan, J.,Gao, G.F.,Wang, Q.
Broad host range of SARS-CoV-2 and the molecular basis for SARS-CoV-2 binding to cat ACE2.
Cell Discov, 6:68-68, 2020

PubMed Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of the recent pandemic COVID-19, is reported to have originated from bats, with its intermediate host unknown to date. Here, we screened 26 animal counterparts of the human ACE2 (hACE2), the receptor for SARS-CoV-2 and SARS-CoV, and found that the ACE2s from various species, including pets, domestic animals and multiple wild animals, could bind to SARS-CoV-2 receptor binding domain (RBD) and facilitate the transduction of SARS-CoV-2 pseudovirus. Comparing to SARS-CoV-2, SARS-CoV seems to have a slightly wider range in choosing its receptor. We further resolved the cryo-electron microscopy (cryo-EM) structure of the cat ACE2 (cACE2) in complex with the SARS-CoV-2 RBD at a resolution of 3 Å, revealing similar binding mode as hACE2 to the SARS-CoV-2 RBD. These results shed light on pursuing the intermediate host of SARS-CoV-2 and highlight the necessity of monitoring susceptible hosts to prevent further outbreaks.

PubMed: 33020722
DOI: 10.1038/s41421-020-00210-9

Experimental method

ELECTRON MICROSCOPY (3 Å)