8SUZ
Open State of the SARS-CoV-2 Envelope Protein Transmembrane Domain, Determined by Solid-State NMR
Summary for 8SUZ
| Entry DOI | 10.2210/pdb8suz/pdb |
| NMR Information | BMRB: 31085 |
| Descriptor | Envelope small membrane protein (1 entity in total) |
| Functional Keywords | viroporin, sars-cov-2, cation channel, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 |
| Total number of polymer chains | 5 |
| Total formula weight | 16810.57 |
| Authors | Medeiros-Silva, J.,Dregni, A.J.,Somberg, N.H.,Hong, M. (deposition date: 2023-05-14, release date: 2023-10-25, Last modification date: 2024-05-15) |
| Primary citation | Medeiros-Silva, J.,Dregni, A.J.,Somberg, N.H.,Duan, P.,Hong, M. Atomic structure of the open SARS-CoV-2 E viroporin. Sci Adv, 9:eadi9007-eadi9007, 2023 Cited by PubMed Abstract: The envelope (E) protein of the SARS-CoV-2 virus forms cation-conducting channels in the endoplasmic reticulum Golgi intermediate compartment (ERGIC) of infected cells. The calcium channel activity of E is associated with the inflammatory responses of COVID-19. Using solid-state NMR (ssNMR) spectroscopy, we have determined the open-state structure of E's transmembrane domain (ETM) in lipid bilayers. Compared to the closed state, open ETM has an expansive water-filled amino-terminal chamber capped by key glutamate and threonine residues, a loose phenylalanine aromatic belt in the middle, and a constricted polar carboxyl-terminal pore filled with an arginine and a threonine residue. This structure gives insights into how protons and calcium ions are selected by ETM and how they permeate across the hydrophobic gate of this viroporin. PubMed: 37831764DOI: 10.1126/sciadv.adi9007 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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