8suz

Open State of the SARS-CoV-2 Envelope Protein Transmembrane Domain, Determined by Solid-State NMR

spinqualitylabelsall models 8suz Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8suz is a 5 chain structure with sequence from Severe acute respiratory syndrome coronavirus 2. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solid-state NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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