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7DRV

Structural basis of SARS-CoV-2-closely-related bat coronavirus RaTG13 to hACE2

Summary for 7DRV
Entry DOI10.2210/pdb7drv/pdb
DescriptorAngiotensin-converting enzyme 2, Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordsratg13, rbd, sars-cov-2, ace2, viral protein, hydrolase-viral protein complex, hydrolase/viral protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains4
Total formula weight190888.08
Authors
Primary citationLiu, K.,Pan, X.,Li, L.,Yu, F.,Zheng, A.,Du, P.,Han, P.,Meng, Y.,Zhang, Y.,Wu, L.,Chen, Q.,Song, C.,Jia, Y.,Niu, S.,Lu, D.,Qiao, C.,Chen, Z.,Ma, D.,Ma, X.,Tan, S.,Zhao, X.,Qi, J.,Gao, G.F.,Wang, Q.
Binding and molecular basis of the bat coronavirus RaTG13 virus to ACE2 in humans and other species.
Cell, 184:3438-3451.e10, 2021
Cited by
PubMed Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has been spreading worldwide, causing a global pandemic. Bat-origin RaTG13 is currently the most phylogenetically related virus. Here we obtained the complex structure of the RaTG13 receptor binding domain (RBD) with human ACE2 (hACE2) and evaluated binding of RaTG13 RBD to 24 additional ACE2 orthologs. By substituting residues in the RaTG13 RBD with their counterparts in the SARS-CoV-2 RBD, we found that residue 501, the major position found in variants of concern (VOCs) 501Y.V1/V2/V3, plays a key role in determining the potential host range of RaTG13. We also found that SARS-CoV-2 could induce strong cross-reactive antibodies to RaTG13 and identified a SARS-CoV-2 monoclonal antibody (mAb), CB6, that could cross-neutralize RaTG13 pseudovirus. These results elucidate the receptor binding and host adaption mechanisms of RaTG13 and emphasize the importance of continuous surveillance of coronaviruses (CoVs) carried by animal reservoirs to prevent another spillover of CoVs.
PubMed: 34139177
DOI: 10.1016/j.cell.2021.05.031
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.09 Å)
Structure validation

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