7VGR
SARS-CoV-2 M protein dimer (long form) in complex with YN7756_1 Fab
Summary for 7VGR
Entry DOI | 10.2210/pdb7vgr/pdb |
EMDB information | 31977 |
Descriptor | YN7756_1 Fab light chain, YN7756_1 Fab heavy chain, Membrane protein (3 entities in total) |
Functional Keywords | sars-cov-2, m protein, viral structural protein, virus assembly, viral protein, viral protein-immune system complex, viral protein/immune system |
Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2) More |
Total number of polymer chains | 6 |
Total formula weight | 154794.69 |
Authors | Zhang, Z.,Ohto, U.,Shimizu, T. (deposition date: 2021-09-18, release date: 2022-08-03, Last modification date: 2024-10-30) |
Primary citation | 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. Structure of SARS-CoV-2 membrane protein essential for virus assembly. Nat Commun, 13:4399-4399, 2022 Cited by PubMed Abstract: 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. PubMed: 35931673DOI: 10.1038/s41467-022-32019-3 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.7 Å) |
Structure validation
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