7VXB
SARS-CoV-2 Kappa variant spike protein in C2b state
Summary for 7VXB
| Entry DOI | 10.2210/pdb7vxb/pdb |
| EMDB information | 32174 |
| Descriptor | Spike glycoprotein, Angiotensin-converting enzyme 2 (2 entities in total) |
| Functional Keywords | sars-cov-2, coronavirus, kappa variant, b.1.617.1 lineage, spike protein, viral protein, viral protein-hydrolase complex, viral protein/hydrolase |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2) More |
| Total number of polymer chains | 4 |
| Total formula weight | 492873.82 |
| Authors | |
| Primary citation | Wang, Y.,Xu, C.,Wang, Y.,Hong, Q.,Zhang, C.,Li, Z.,Xu, S.,Zuo, Q.,Liu, C.,Huang, Z.,Cong, Y. Conformational dynamics of the Beta and Kappa SARS-CoV-2 spike proteins and their complexes with ACE2 receptor revealed by cryo-EM. Nat Commun, 12:7345-7345, 2021 Cited by PubMed Abstract: The emergence of SARS-CoV-2 Kappa and Beta variants with enhanced transmissibility and resistance to neutralizing antibodies has created new challenges for the control of the ongoing COVID-19 pandemic. Understanding the structural nature of Kappa and Beta spike (S) proteins and their association with ACE2 is of significant importance. Here we present two cryo-EM structures for each of the Kappa and Beta spikes in the open and open-prone transition states. Compared with wild-type (WT) or G614 spikes, the two variant spikes appear more untwisted/open especially for Beta, and display a considerable population shift towards the open state as well as more pronounced conformational dynamics. Moreover, we capture four conformational states of the S-trimer/ACE2 complex for each of the two variants, revealing an enlarged conformational landscape for the Kappa and Beta S-ACE2 complexes and pronounced population shift towards the three RBDs up conformation. These results implicate that the mutations in Kappa and Beta may modify the kinetics of receptor binding and viral fusion to improve virus fitness. Combined with biochemical analysis, our structural study shows that the two variants are enabled to efficiently interact with ACE2 receptor despite their sensitive ACE2 binding surface is modified to escape recognition by some potent neutralizing MAbs. Our findings shed new light on the pathogenicity and immune evasion mechanism of the Beta and Kappa variants. PubMed: 34930910DOI: 10.1038/s41467-021-27350-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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