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| | ==NMR structure of the SARS Coronavirus E protein pentameric ion channel== | | ==NMR structure of the SARS Coronavirus E protein pentameric ion channel== |
| - | <StructureSection load='5x29' size='340' side='right' caption='[[5x29]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''> | + | <StructureSection load='5x29' size='340' side='right'caption='[[5x29]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5x29]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Cvhsa Cvhsa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X29 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X29 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5x29]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome-related_coronavirus Severe acute respiratory syndrome-related coronavirus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X29 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mm4|2mm4]]</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5x29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x29 OCA], [https://pdbe.org/5x29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x29 RCSB], [https://www.ebi.ac.uk/pdbsum/5x29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x29 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">E, sM, 4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=227859 CVHSA])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5x29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x29 OCA], [http://pdbe.org/5x29 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x29 RCSB], [http://www.ebi.ac.uk/pdbsum/5x29 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x29 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/VEMP_CVHSA VEMP_CVHSA]] Component of the viral envelope that plays a central role in virus morphogenesis and assembly. It is sufficient to form virus-like particles. Seems to be important for creating the membrane curvature needed to acquire the rounded, stable and infectious particle phenotype. Acts as a viroporin, inducing the formation of hydrophilic pores in cellular membranes. Also induces apoptosis (By similarity). | + | [https://www.uniprot.org/uniprot/VEMP_SARS 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]<ref>PMID:24788150</ref> <ref>PMID:26331680</ref> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == 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<ref>PMID:29474890</ref> |
| | + | |
| | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | + | </div> |
| | + | <div class="pdbe-citations 5x29" style="background-color:#fffaf0;"></div> |
| | + | == References == |
| | + | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cvhsa]] | + | [[Category: Large Structures]] |
| - | [[Category: Li, Y]] | + | [[Category: Severe acute respiratory syndrome-related coronavirus]] |
| - | [[Category: Surya, W]] | + | [[Category: Li Y]] |
| - | [[Category: Torres, J]] | + | [[Category: Surya W]] |
| - | [[Category: Envelope protein]] | + | [[Category: Torres J]] |
| - | [[Category: Ion channel]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Pentamer]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
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
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