7VGR

SARS-CoV-2 M protein dimer (long form) in complex with YN7756_1 Fab

7VGR の概要

• エントリーDOI: 10.2210/pdb7vgr/pdb
• EMDBエントリー: 31977
• 分子名称: YN7756_1 Fab light chain, YN7756_1 Fab heavy chain, Membrane protein (3 entities in total)
• 機能のキーワード: sars-cov-2, m protein, viral structural protein, virus assembly, viral protein, viral protein-immune system complex, viral protein/immune system
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 154794.69

構造登録者

Zhang, Z.,Ohto, U.,Shimizu, T. (登録日: 2021-09-18, 公開日: 2022-08-03, 最終更新日: 2025-06-25)

主引用文献

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

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: 35931673
DOI: 10.1038/s41467-022-32019-3

実験手法

ELECTRON MICROSCOPY (2.7 Å)