7XBY

The crystal structure of SARS-CoV-2 Omicron BA.1 variant RBD in complex with equine ACE2

Summary for 7XBY

• Entry DOI: 10.2210/pdb7xby/pdb
• Descriptor: Angiotensin-converting enzyme, Spike protein S1, ZINC ION, ... (5 entities in total)
• Functional Keywords: complex, viral protein
• Biological source: Equus caballus (horse); More
• Total number of polymer chains: 2
• Total formula weight: 118481.01

Authors

Xu, Z.P.,Liu, K.F.,Han, P.,Qi, J.X. (deposition date: 2022-03-22, release date: 2022-06-08, Last modification date: 2024-11-13)

Primary citation

Xu, Z.,Kang, X.,Han, P.,Du, P.,Li, L.,Zheng, A.,Deng, C.,Qi, J.,Zhao, X.,Wang, Q.,Liu, K.,Gao, G.F.
Binding and structural basis of equine ACE2 to RBDs from SARS-CoV, SARS-CoV-2 and related coronaviruses.
Nat Commun, 13:3547-3547, 2022

PubMed Abstract: The origin and host range of SARS-CoV-2, the causative agent of coronavirus disease 2019 (COVID-19), are important scientific questions as they might provide insight into understanding of the potential future spillover to infect humans. Here, we tested the binding between equine angiotensin converting enzyme 2 (eqACE2) and the receptor binding domains (RBDs) of SARS-CoV, SARS-CoV-2 prototype (PT) and variant of concerns (VOCs), as well as their close relatives bat-origin coronavirus (CoV) RaTG13 and pangolin-origin CoVs GX/P2V/2017 and GD/1/2019. We also determined the crystal structures of eqACE2/RaTG13-RBD, eqACE2/SARS-CoV-2 PT-RBD and eqACE2/Omicron BA.1-RBD. We identified S494 of SARS-COV-2 PT-RBD as an important residue in the eqACE2/SARS-COV-2 PT-RBD interaction and found that N501Y, the commonly recognized enhancing mutation, attenuated the binding affinity with eqACE2. Our work demonstrates that horses are potential targets for SARS-CoV-2 and highlights the importance of continuous surveillance on SARS-CoV-2 and related CoVs to prevent spillover events.

PubMed: 35729237
DOI: 10.1038/s41467-022-31276-6

Experimental method

X-RAY DIFFRACTION (2.85 Å)