This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5x29

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5x29"

Categories: Large Structures | Severe acute respiratory syndrome-related coronavirus | Li Y | Surya W | Torres J

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5x29 is ON HOLD  until Paper Publication
+==NMR structure of the SARS Coronavirus E protein pentameric ion channel==
+<StructureSection load='5x29' size='340' side='right'caption='[[5x29]]' scene=''>
+== Structural highlights ==
+<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='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>
+</table>
+== Function ==
+[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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5x29" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Severe acute respiratory syndrome-related coronavirus]]
+[[Category: Li Y]]
+[[Category: Surya W]]
+[[Category: Torres J]]

5x29

From Proteopedia

Current revision

NMR structure of the SARS Coronavirus E protein pentameric ion channel

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox