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5x29

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NMR structure of the SARS Coronavirus E protein pentameric ion channel

Structural highlights

5x29 is a 5 chain structure with sequence from Severe acute respiratory syndrome-related coronavirus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VEMP_SARS 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 (By similarity). Activates the host NLRP3 inflammasome, leading to IL-1beta overproduction.[HAMAP-Rule:MF_04204]^[1] ^[2]

Publication Abstract from PubMed

Coronaviruses (CoV) cause common colds in humans, but are also responsible for the recent Severe Acute, and Middle East, respiratory syndromes (SARS and MERS, respectively). A promising approach for prevention are live attenuated vaccines (LAVs), some of which target the envelope (E) protein, which is a small membrane protein that forms ion channels. Unfortunately, detailed structural information is still limited for SARS-CoV E, and non-existent for other CoV E proteins. Herein, we report a structural model of a SARS-CoV E construct in LMPG micelles with, for the first time, unequivocal intermolecular NOEs. The model corresponding to the detergent-embedded region is consistent with previously obtained orientational restraints obtained in lipid bilayers and in vivo escape mutants. The C-terminal domain is mostly alpha-helical, and extramembrane intermolecular NOEs suggest interactions that may affect the TM channel conformation.

Structural model of the SARS coronavirus E channel in LMPG micelles.,Surya W, Li Y, Torres J Biochim Biophys Acta. 2018 Jun;1860(6):1309-1317. doi:, 10.1016/j.bbamem.2018.02.017. Epub 2018 Feb 21. PMID:29474890^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nieto-Torres JL, DeDiego ML, Verdiá-Báguena C, Jimenez-Guardeño JM, Regla-Nava JA, Fernandez-Delgado R, Castaño-Rodriguez C, Alcaraz A, Torres J, Aguilella VM, Enjuanes L. Severe acute respiratory syndrome coronavirus envelope protein ion channel activity promotes virus fitness and pathogenesis. PLoS Pathog. 2014 May 1;10(5):e1004077. PMID:24788150 doi:10.1371/journal.ppat.1004077
↑ Nieto-Torres JL, Verdiá-Báguena C, Jimenez-Guardeño JM, Regla-Nava JA, Castaño-Rodriguez C, Fernandez-Delgado R, Torres J, Aguilella VM, Enjuanes L. Severe acute respiratory syndrome coronavirus E protein transports calcium ions and activates the NLRP3 inflammasome. Virology. 2015 Nov;485:330-9. PMID:26331680 doi:10.1016/j.virol.2015.08.010
↑ Surya W, Li Y, Torres J. Structural model of the SARS coronavirus E channel in LMPG micelles. Biochim Biophys Acta. 2018 Jun;1860(6):1309-1317. doi:, 10.1016/j.bbamem.2018.02.017. Epub 2018 Feb 21. PMID:29474890 doi:http://dx.doi.org/10.1016/j.bbamem.2018.02.017