7K3G
SARS-CoV-2 Envelope Protein Transmembrane Domain: Pentameric Structure Determined by Solid-State NMR
Summary for 7K3G
| Entry DOI | 10.2210/pdb7k3g/pdb |
| NMR Information | BMRB: 30795 |
| Descriptor | Envelope small membrane protein (1 entity in total) |
| Functional Keywords | viroporin, pentameric ion channel, transmembrane domain, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) |
| Total number of polymer chains | 5 |
| Total formula weight | 16810.57 |
| Authors | Mandala, V.S.,Hong, M.,McKay, M.J.,Shcherbakov, A.S.,Dregni, A.J. (deposition date: 2020-09-11, release date: 2020-09-30, Last modification date: 2024-05-15) |
| Primary citation | Mandala, V.S.,McKay, M.J.,Shcherbakov, A.A.,Dregni, A.J.,Kolocouris, A.,Hong, M. Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers. Nat.Struct.Mol.Biol., 27:1202-1208, 2020 Cited by PubMed Abstract: An essential protein of the SARS-CoV-2 virus, the envelope protein E, forms a homopentameric cation channel that is important for virus pathogenicity. Here we report a 2.1-Å structure and the drug-binding site of E's transmembrane domain (ETM), determined using solid-state NMR spectroscopy. In lipid bilayers that mimic the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membrane, ETM forms a five-helix bundle surrounding a narrow pore. The protein deviates from the ideal α-helical geometry due to three phenylalanine residues, which stack within each helix and between helices. Together with valine and leucine interdigitation, these cause a dehydrated pore compared with the viroporins of influenza viruses and HIV. Hexamethylene amiloride binds the polar amino-terminal lumen, whereas acidic pH affects the carboxy-terminal conformation. Thus, the N- and C-terminal halves of this bipartite channel may interact with other viral and host proteins semi-independently. The structure sets the stage for designing E inhibitors as antiviral drugs. PubMed: 33177698DOI: 10.1038/s41594-020-00536-8 PDB entries with the same primary citation |
| Experimental method | SOLID-STATE NMR |
Structure validation
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