View source for 2mm4


==Structure of a Conserved Golgi Complex-targeting Signal in Coronavirus Envelope Proteins==
<StructureSection load='2mm4' size='340' side='right'caption='[[2mm4]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mm4]] is a 1 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=2MM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MM4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mm4 OCA], [https://pdbe.org/2mm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mm4 RCSB], [https://www.ebi.ac.uk/pdbsum/2mm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mm4 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> 
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== Publication Abstract from PubMed ==
Coronavirus envelope (CoV E) proteins are approximately 100-residue polypeptides with at least one channel-forming alpha-helical transmembrane (TM) domain. The extramembrane C-terminal tail contains a completely conserved proline, at the center of a predicted beta-coil-beta motif. This hydrophobic motif has been reported to constitute a Golgi-targeting signal or a second TM domain. However, no structural data for this or other extramembrane domains in CoV E proteins is available. Herein, we show that the E protein in the severe acute respiratory syndrome virus has only one TM domain in micelles, whereas the predicted beta-coil-beta motif forms a short membrane-bound alpha-helix connected by a disordered loop to the TM domain. However, complementary results suggest that this motif is potentially poised for conformational change or in dynamic exchange with other conformations.

Structure of a conserved Golgi complex-targeting signal in coronavirus envelope proteins.,Li Y, Surya W, Claudine S, Torres J J Biol Chem. 2014 May 2;289(18):12535-49. doi: 10.1074/jbc.M114.560094. Epub 2014, Mar 25. PMID:24668816<ref>PMID:24668816</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Severe acute respiratory syndrome-related coronavirus]]
[[Category: Claudine S]]
[[Category: Li Y]]
[[Category: Surya W]]
[[Category: Torres J]]