Atomic structure of the open SARS-CoV-2 E viroporin
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sciadv.adi9007.pdf
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2.44 MB
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Adobe PDF
Checksum (MD5)
6eb5b40152f57f595135967440587309
Author(s)
Medeiros-Silva, João
Dregni, Aurelio J.
Somberg, Noah H.
Duan, Pu
Hong, Mei
Date Issued
October 13, 2023
Publisher
American Association for the Advancement of Science
Citation
João Medeiros-Silva et al. ,Atomic structure of the open SARS-CoV-2 E viroporin.Sci. Adv.9,eadi9007(2023).
Version
Final published version
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.
Subjects
Multidisciplinary
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Creative Commons Attribution
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DOI of Published Version
https://doi.org/10.1126/sciadv.adi9007
