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| | ==SARS-CoV-2 Envelope Protein Transmembrane Domain: Pentameric Structure Determined by Solid-State NMR== | | ==SARS-CoV-2 Envelope Protein Transmembrane Domain: Pentameric Structure Determined by Solid-State NMR== |
| - | <StructureSection load='7k3g' size='340' side='right'caption='[[7k3g]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='7k3g' size='340' side='right'caption='[[7k3g]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7k3g]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/2019-ncov 2019-ncov]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K3G OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7K3G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7k3g]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome_coronavirus_2 Severe acute respiratory syndrome coronavirus 2]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K3G FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">E, 4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2697049 2019-nCoV])</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7k3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k3g OCA], [https://pdbe.org/7k3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k3g RCSB], [https://www.ebi.ac.uk/pdbsum/7k3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k3g ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7k3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k3g OCA], [http://pdbe.org/7k3g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7k3g RCSB], [http://www.ebi.ac.uk/pdbsum/7k3g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7k3g ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/VEMP_SARS2 VEMP_SARS2]] Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis.[HAMAP-Rule:MF_04204] | + | [https://www.uniprot.org/uniprot/VEMP_SARS2 VEMP_SARS2] Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis.[HAMAP-Rule:MF_04204] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 2019-ncov]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dregni, A J]] | + | [[Category: Severe acute respiratory syndrome coronavirus 2]] |
| - | [[Category: Hong, M]] | + | [[Category: Dregni AJ]] |
| - | [[Category: Mandala, V S]] | + | [[Category: Hong M]] |
| - | [[Category: McKay, M J]]
| + | [[Category: Mandala VS]] |
| - | [[Category: Shcherbakov, A S]] | + | [[Category: McKay MJ]] |
| - | [[Category: Pentameric ion channel]] | + | [[Category: Shcherbakov AS]] |
| - | [[Category: Transmembrane domain]] | + | |
| - | [[Category: Viral protein]]
| + | |
| - | [[Category: Viroporin]]
| + | |
| Structural highlights
Function
VEMP_SARS2 Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis.[HAMAP-Rule:MF_04204]
Publication Abstract from PubMed
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-A 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 alpha-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.
Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers.,Mandala VS, McKay MJ, Shcherbakov AA, Dregni AJ, Kolocouris A, Hong M Nat Struct Mol Biol. 2020 Nov 11. pii: 10.1038/s41594-020-00536-8. doi:, 10.1038/s41594-020-00536-8. PMID:33177698[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mandala VS, McKay MJ, Shcherbakov AA, Dregni AJ, Kolocouris A, Hong M. Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers. Nat Struct Mol Biol. 2020 Nov 11. pii: 10.1038/s41594-020-00536-8. doi:, 10.1038/s41594-020-00536-8. PMID:33177698 doi:http://dx.doi.org/10.1038/s41594-020-00536-8
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