6ACG
Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-bound conformation 1
Summary for 6ACG
| Entry DOI | 10.2210/pdb6acg/pdb |
| EMDB information | 9588 9589 9591 |
| Descriptor | Spike glycoprotein, Angiotensin-converting enzyme 2 (2 entities in total) |
| Functional Keywords | sars-cov, spike, glycoprotein, class i fusion protein, membrane fusion, viral protein, viral protein-hydrolase complex, viral protein/hydrolase |
| Biological source | Human SARS coronavirus (SARS-CoV) More |
| Total number of polymer chains | 4 |
| Total formula weight | 471272.83 |
| Authors | |
| Primary citation | Song, W.,Gui, M.,Wang, X.,Xiang, Y. Cryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2. PLoS Pathog., 14:e1007236-e1007236, 2018 Cited by PubMed Abstract: The trimeric SARS coronavirus (SARS-CoV) surface spike (S) glycoprotein consisting of three S1-S2 heterodimers binds the cellular receptor angiotensin-converting enzyme 2 (ACE2) and mediates fusion of the viral and cellular membranes through a pre- to postfusion conformation transition. Here, we report the structure of the SARS-CoV S glycoprotein in complex with its host cell receptor ACE2 revealed by cryo-electron microscopy (cryo-EM). The complex structure shows that only one receptor-binding domain of the trimeric S glycoprotein binds ACE2 and adopts a protruding "up" conformation. In addition, we studied the structures of the SARS-CoV S glycoprotein and its complexes with ACE2 in different in vitro conditions, which may mimic different conformational states of the S glycoprotein during virus entry. Disassociation of the S1-ACE2 complex from some of the prefusion spikes was observed and characterized. We also characterized the rosette-like structures of the clustered SARS-CoV S2 trimers in the postfusion state observed on electron micrographs. Structural comparisons suggested that the SARS-CoV S glycoprotein retains a prefusion architecture after trypsin cleavage into the S1 and S2 subunits and acidic pH treatment. However, binding to the receptor opens up the receptor-binding domain of S1, which could promote the release of the S1-ACE2 complex and S1 monomers from the prefusion spike and trigger the pre- to postfusion conformational transition. PubMed: 30102747DOI: 10.1371/journal.ppat.1007236 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (5.4 Å) |
Structure validation
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