8SUZ

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

8SUZ の概要

• エントリーDOI: 10.2210/pdb8suz/pdb
• NMR情報: BMRB: 31085
• 分子名称: Envelope small membrane protein (1 entity in total)
• 機能のキーワード: viroporin, sars-cov-2, cation channel, viral protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 16810.57

構造登録者

Medeiros-Silva, J.,Dregni, A.J.,Somberg, N.H.,Hong, M. (登録日: 2023-05-14, 公開日: 2023-10-25, 最終更新日: 2024-05-15)

主引用文献

Medeiros-Silva, J.,Dregni, A.J.,Somberg, N.H.,Duan, P.,Hong, M.
Atomic structure of the open SARS-CoV-2 E viroporin.
Sci Adv, 9:eadi9007-eadi9007, 2023

PubMed 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.

PubMed: 37831764
DOI: 10.1126/sciadv.adi9007

実験手法

SOLID-STATE NMR