2mm4

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==Structure of a Conserved Golgi Complex-targeting Signal in Coronavirus Envelope Proteins==
==Structure of a Conserved Golgi Complex-targeting Signal in Coronavirus Envelope Proteins==
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<StructureSection load='2mm4' size='340' side='right' caption='[[2mm4]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
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<StructureSection load='2mm4' size='340' side='right'caption='[[2mm4]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2mm4]] is a 1 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=2MM4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MM4 FirstGlance]. <br>
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<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>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=227859 CVHSA])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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=2mm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mm4 OCA], [http://pdbe.org/2mm4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mm4 RCSB], [http://www.ebi.ac.uk/pdbsum/2mm4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mm4 ProSAT]</span></td></tr>
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<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>
</table>
== Function ==
== Function ==
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[[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).
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[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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2mm4" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cvhsa]]
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[[Category: Large Structures]]
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[[Category: Claudine, S]]
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[[Category: Severe acute respiratory syndrome-related coronavirus]]
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[[Category: Li, Y]]
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[[Category: Claudine S]]
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[[Category: Surya, W]]
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[[Category: Li Y]]
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[[Category: Torres, J]]
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[[Category: Surya W]]
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[[Category: Envelope protein]]
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[[Category: Torres J]]
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[[Category: Membrane protein]]
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[[Category: Sars coronavirus]]
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[[Category: Viral protein]]
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Current revision

Structure of a Conserved Golgi Complex-targeting Signal in Coronavirus Envelope Proteins

PDB ID 2mm4

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