7JM3
Full-length three-dimensional structure of the influenza A virus M1 protein and its organization into a matrix layer
Summary for 7JM3
| Entry DOI | 10.2210/pdb7jm3/pdb |
| EMDB information | 22384 |
| Descriptor | Matrix protein 1 (1 entity in total) |
| Functional Keywords | influenza a, virus, matrix layer, m1 protein, viral protein |
| Biological source | Influenza A virus (strain A/Puerto Rico/8/1934 H1N1) |
| Total number of polymer chains | 1 |
| Total formula weight | 27827.15 |
| Authors | Su, Z.,Pintilie, G.,Selzer, L.,Chiu, W.,Kirkegaard, K. (deposition date: 2020-07-30, release date: 2020-08-12, Last modification date: 2024-03-06) |
| Primary citation | Selzer, L.,Su, Z.,Pintilie, G.D.,Chiu, W.,Kirkegaard, K. Full-length three-dimensional structure of the influenza A virus M1 protein and its organization into a matrix layer. Plos Biol., 18:e3000827-e3000827, 2020 Cited by PubMed Abstract: Matrix proteins are encoded by many enveloped viruses, including influenza viruses, herpes viruses, and coronaviruses. Underneath the viral envelope of influenza virus, matrix protein 1 (M1) forms an oligomeric layer critical for particle stability and pH-dependent RNA genome release. However, high-resolution structures of full-length monomeric M1 and the matrix layer have not been available, impeding antiviral targeting and understanding of the pH-dependent transitions involved in cell entry. Here, purification and extensive mutagenesis revealed protein-protein interfaces required for the formation of multilayered helical M1 oligomers similar to those observed in virions exposed to the low pH of cell entry. However, single-layered helical oligomers with biochemical and ultrastructural similarity to those found in infectious virions before cell entry were observed upon mutation of a single amino acid. The highly ordered structure of the single-layered oligomers and their likeness to the matrix layer of intact virions prompted structural analysis by cryo-electron microscopy (cryo-EM). The resulting 3.4-Å-resolution structure revealed the molecular details of M1 folding and its organization within the single-shelled matrix. The solution of the full-length M1 structure, the identification of critical assembly interfaces, and the development of M1 assembly assays with purified proteins are crucial advances for antiviral targeting of influenza viruses. PubMed: 32997652DOI: 10.1371/journal.pbio.3000827 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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