|Title||Cryo-EM structure of the SARS-CoV-2 3a ion channel in lipid nanodiscs.|
|Journal, issue, pages||bioRxiv, Year 2020|
|Publish date||Jun 18, 2020|
|Authors||David M Kern / Ben Sorum / Christopher M Hoel / Savitha Sridharan / Jonathan P Remis / Daniel B Toso / Stephen G Brohawn|
|PubMed Abstract||SARS-CoV-2 encodes three putative ion channels: E, 8a, and 3a. In related SARS-CoV-1, 3a is implicated in viral release, inflammasome activation, and cell death and its deletion reduces viral titer ...SARS-CoV-2 encodes three putative ion channels: E, 8a, and 3a. In related SARS-CoV-1, 3a is implicated in viral release, inflammasome activation, and cell death and its deletion reduces viral titer and morbidity in animal models, suggesting 3a-targeted therapeutics could treat SARS and COVID-19. However, the structural basis for the function of 3a is unknown. Here, we show that SARS-CoV-2 forms large conductance cation channels and present cryo-EM structures of dimeric and tetrameric SARS-CoV-2 3a in lipid nanodiscs. 3a adopts a novel fold and is captured in a closed or inactivated state. A narrow bifurcated exterior pore precludes conduction and leads to a large polar cavity open to the cytosol. 3a function is conserved in a common variant among circulating SARS-CoV-2 that alters the channel pore. We identify 3a-like proteins in and that infect bats and humans, suggesting therapeutics targeting 3a could treat a range of coronaviral diseases.|
|External links||PubMed:32587976 / Publisher's page|
|Keywords||TRANSPORT PROTEIN / SARS-CoV-2 / coronavirus / viroporin / ion channel|
|Methods||EM (single particle)|
|Resolution||2.9 - 6.5 A|
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