From Proteopedia
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| + | '''Unreleased structure''' |
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- | ==SARS-CoV-2 Envelope Protein Transmembrane Domain: Dimeric Structure Determined by Solid-State NMR==
| + | The entry 8u1t is ON HOLD until Paper Publication |
- | <StructureSection load='8u1t' size='340' side='right'caption='[[8u1t]]' scene=''>
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- | == Structural highlights ==
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- | <table><tr><td colspan='2'>[[8u1t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome_coronavirus_2 Severe acute respiratory syndrome coronavirus 2]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8U1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8U1T FirstGlance]. <br>
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- | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</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=8u1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8u1t OCA], [https://pdbe.org/8u1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8u1t RCSB], [https://www.ebi.ac.uk/pdbsum/8u1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8u1t ProSAT]</span></td></tr>
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- | </table>
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- | == Function ==
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- | [https://www.uniprot.org/uniprot/VEMP_SARS2 VEMP_SARS2] 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.[HAMAP-Rule:MF_04204]
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- | <div style="background-color:#fffaf0;">
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- | == Publication Abstract from PubMed ==
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- | The SARS-CoV-2 E protein is a transmembrane (TM) protein with its N-terminus exposed on the external surface of the virus. At debate is its oligomeric state, let alone its function. Here, the TM structure of the E protein is characterized by oriented sample and magic angle spinning solid-state NMR in lipid bilayers and refined by molecular dynamics simulations. This protein was previously found to be a pentamer, with a hydrophobic pore that appears to function as an ion channel. We identify only a front-to-front, symmetric helix-helix interface, leading to a dimeric structure that does not support channel activity. The two helices have a tilt angle of only 6 degrees , resulting in an extended interface dominated by Leu and Val sidechains. While residues Val14-Thr35 are almost all buried in the hydrophobic region of the membrane, Asn15 lines a water-filled pocket that potentially serves as a drug-binding site. The E and other viral proteins may adopt different oligomeric states to help perform multiple functions.
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- | Dimeric Transmembrane Structure of the SARS-CoV-2 E Protein.,Zhang R, Qin H, Prasad R, Fu R, Zhou HX, Cross TA Commun Biol. 2023 Nov 1;6(1):1109. doi: 10.1038/s42003-023-05490-x. PMID:37914906<ref>PMID:37914906</ref>
| + | Authors: Zhang, R., Qin, H., Prasad, R., Fu, R., Zhou, H.X., Cross, T. |
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | Description: SARS-CoV-2 Envelope Protein Transmembrane Domain: Dimeric Structure Determined by Solid-State NMR |
- | </div>
| + | [[Category: Unreleased Structures]] |
- | <div class="pdbe-citations 8u1t" style="background-color:#fffaf0;"></div>
| + | [[Category: Zhou, H.X]] |
- | == References ==
| + | [[Category: Zhang, R]] |
- | <references/>
| + | [[Category: Qin, H]] |
- | __TOC__
| + | [[Category: Prasad, R]] |
- | </StructureSection>
| + | [[Category: Cross, T]] |
- | [[Category: Large Structures]] | + | [[Category: Fu, R]] |
- | [[Category: Severe acute respiratory syndrome coronavirus 2]] | + | |
- | [[Category: Cross T]] | + | |
- | [[Category: Fu R]] | + | |
- | [[Category: Prasad R]] | + | |
- | [[Category: Qin H]] | + | |
- | [[Category: Zhang R]] | + | |
- | [[Category: Zhou HX]]
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Current revision
Unreleased structure
The entry 8u1t is ON HOLD until Paper Publication
Authors: Zhang, R., Qin, H., Prasad, R., Fu, R., Zhou, H.X., Cross, T.
Description: SARS-CoV-2 Envelope Protein Transmembrane Domain: Dimeric Structure Determined by Solid-State NMR