7vgs: Difference between revisions

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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=7vgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vgs OCA], [https://pdbe.org/7vgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vgs RCSB], [https://www.ebi.ac.uk/pdbsum/7vgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vgs ProSAT]</span></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=7vgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vgs OCA], [https://pdbe.org/7vgs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vgs RCSB], [https://www.ebi.ac.uk/pdbsum/7vgs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vgs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
<div style="background-color:#fffaf0;">
[https://www.uniprot.org/uniprot/VME1_SARS2 VME1_SARS2] Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins (By similarity). Regulates the localization of S protein at cis-Golgi, the place of virus budding (PubMed:33229438). May act by binding cytoplasmic c-terminus of S (PubMed:33229438).[HAMAP-Rule:MF_04202][PROSITE-ProRule:PRU01275]<ref>PMID:33229438</ref>  
== Publication Abstract from PubMed ==
The coronavirus membrane protein (M) is the most abundant viral structural protein and plays a central role in virus assembly and morphogenesis. However, the process of M protein-driven virus assembly are largely unknown. Here, we report the cryo-electron microscopy structure of the SARS-CoV-2 M protein in two different conformations. M protein forms a mushroom-shaped dimer, composed of two transmembrane domain-swapped three-helix bundles and two intravirion domains. M protein further assembles into higher-order oligomers. A highly conserved hinge region is key for conformational changes. The M protein dimer is unexpectedly similar to SARS-CoV-2 ORF3a, a viral ion channel. Moreover, the interaction analyses of M protein with nucleocapsid protein (N) and RNA suggest that the M protein mediates the concerted recruitment of these components through the positively charged intravirion domain. Our data shed light on the M protein-driven virus assembly mechanism and provide a structural basis for therapeutic intervention targeting M protein.
 
Structure of SARS-CoV-2 membrane protein essential for virus assembly.,Zhang Z, Nomura N, Muramoto Y, Ekimoto T, Uemura T, Liu K, Yui M, Kono N, Aoki J, Ikeguchi M, Noda T, Iwata S, Ohto U, Shimizu T Nat Commun. 2022 Aug 5;13(1):4399. doi: 10.1038/s41467-022-32019-3. PMID:35931673<ref>PMID:35931673</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7vgs" style="background-color:#fffaf0;"></div>
== References ==
== References ==
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Latest revision as of 06:17, 3 July 2025

SARS-CoV-2 M protein dimer (short form) in complex with YN7717_9 Fab

7vgs, resolution 2.80Å

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