7ZH5
SARS CoV Spike protein, Open conformation
Summary for 7ZH5
| Entry DOI | 10.2210/pdb7zh5/pdb |
| EMDB information | 14724 |
| Descriptor | Spike glycoprotein,Fibritin, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | sars-cov, viral protein, spike |
| Biological source | Severe acute respiratory syndrome-related coronavirus More |
| Total number of polymer chains | 3 |
| Total formula weight | 413693.17 |
| Authors | Toelzer, C.,Gupta, K.,Yadav, S.K.N.,Buzas, D.,Borucu, U.,Schaffitzel, C.,Berger, I. (deposition date: 2022-04-05, release date: 2023-02-15, Last modification date: 2024-11-13) |
| Primary citation | Toelzer, C.,Gupta, K.,Yadav, S.K.N.,Hodgson, L.,Williamson, M.K.,Buzas, D.,Borucu, U.,Powers, K.,Stenner, R.,Vasileiou, K.,Garzoni, F.,Fitzgerald, D.,Payre, C.,Gautam, G.,Lambeau, G.,Davidson, A.D.,Verkade, P.,Frank, M.,Berger, I.,Schaffitzel, C. The free fatty acid-binding pocket is a conserved hallmark in pathogenic beta-coronavirus spike proteins from SARS-CoV to Omicron. Sci Adv, 8:eadc9179-eadc9179, 2022 Cited by PubMed Abstract: As coronavirus disease 2019 (COVID-19) persists, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VOCs) emerge, accumulating spike (S) glycoprotein mutations. S receptor binding domain (RBD) comprises a free fatty acid (FFA)-binding pocket. FFA binding stabilizes a locked S conformation, interfering with virus infectivity. We provide evidence that the pocket is conserved in pathogenic β-coronaviruses (β-CoVs) infecting humans. SARS-CoV, MERS-CoV, SARS-CoV-2, and VOCs bind the essential FFA linoleic acid (LA), while binding is abolished by one mutation in common cold-causing HCoV-HKU1. In the SARS-CoV S structure, LA stabilizes the locked conformation, while the open, infectious conformation is devoid of LA. Electron tomography of SARS-CoV-2-infected cells reveals that LA treatment inhibits viral replication, resulting in fewer deformed virions. Our results establish FFA binding as a hallmark of pathogenic β-CoV infection and replication, setting the stage for FFA-based antiviral strategies to overcome COVID-19. PubMed: 36417532DOI: 10.1126/sciadv.adc9179 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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