6Z5J
Arrangement of the matrix protein M1 in influenza A/Hong Kong/1/1968 VLPs (HA,NA,M1,M2)
Summary for 6Z5J
| Entry DOI | 10.2210/pdb6z5j/pdb |
| EMDB information | 11078 |
| Descriptor | Matrix protein 1 (2 entities in total) |
| Functional Keywords | viral matrix protein, membrane binding, ph sensor, polymer, viral protein |
| Biological source | Influenza A virus (A/Puerto Rico/8-9NMC3/1934(H1N1)) |
| Total number of polymer chains | 6 |
| Total formula weight | 167569.81 |
| Authors | Peukes, J.,Xiong, X.,Erlendsson, S.,Qu, K.,Wan, W.,Kraeusslich, H.-G.,Briggs, J.A.G. (deposition date: 2020-05-26, release date: 2020-10-14, Last modification date: 2024-05-22) |
| Primary citation | Peukes, J.,Xiong, X.,Erlendsson, S.,Qu, K.,Wan, W.,Calder, L.J.,Schraidt, O.,Kummer, S.,Freund, S.M.V.,Krausslich, H.G.,Briggs, J.A.G. The native structure of the assembled matrix protein 1 of influenza A virus. Nature, 587:495-498, 2020 Cited by PubMed Abstract: Influenza A virus causes millions of severe cases of disease during annual epidemics. The most abundant protein in influenza virions is matrix protein 1 (M1), which mediates virus assembly by forming an endoskeleton beneath the virus membrane. The structure of full-length M1, and how it oligomerizes to mediate the assembly of virions, is unknown. Here we determine the complete structure of assembled M1 within intact virus particles, as well as the structure of M1 oligomers reconstituted in vitro. We find that the C-terminal domain of M1 is disordered in solution but can fold and bind in trans to the N-terminal domain of another M1 monomer, thus polymerizing M1 into linear strands that coat the interior surface of the membrane of the assembling virion. In the M1 polymer, five histidine residues-contributed by three different monomers of M1-form a cluster that can serve as the pH-sensitive disassembly switch after entry into a target cell. These structures therefore reveal mechanisms of influenza virus assembly and disassembly. PubMed: 32908308DOI: 10.1038/s41586-020-2696-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (8 Å) |
Structure validation
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