8suz
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Open State of the SARS-CoV-2 Envelope Protein Transmembrane Domain, Determined by Solid-State NMR== | |
| + | <StructureSection load='8suz' size='340' side='right'caption='[[8suz]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8suz]] 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=8SUZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SUZ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</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=8suz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8suz OCA], [https://pdbe.org/8suz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8suz RCSB], [https://www.ebi.ac.uk/pdbsum/8suz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8suz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | Atomic structure of the open SARS-CoV-2 E viroporin.,Medeiros-Silva J, Dregni AJ, Somberg NH, Duan P, Hong M Sci Adv. 2023 Oct 13;9(41):eadi9007. doi: 10.1126/sciadv.adi9007. Epub 2023 Oct , 13. PMID:37831764<ref>PMID:37831764</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8suz" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Severe acute respiratory syndrome coronavirus 2]] | ||
| + | [[Category: Dregni AJ]] | ||
| + | [[Category: Hong M]] | ||
| + | [[Category: Medeiros-Silva J]] | ||
| + | [[Category: Somberg NH]] | ||
Current revision
Open State of the SARS-CoV-2 Envelope Protein Transmembrane Domain, Determined by Solid-State NMR
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