6Z5L

Helical reconstruction of influenza A virus M1 in complex with nucleic acid.


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.80 Å
  • Aggregation State: HELICAL ARRAY 
  • Reconstruction Method: HELICAL 

wwPDB Validation 3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

The native structure of the assembled matrix protein 1 of influenza A virus.

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.

(2020) Nature 

  • DOI: 10.1038/s41586-020-2696-8
  • Primary Citation of Related Structures:  
    6Z5J, 6Z5L

  • 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 1 ...

    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 1 . 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.


    Related Citations: 
    • The native structure of the full-length, assembled influenza A virus matrix protein, M1.
      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.
      (2020) Biorxiv --: --

    Organizational Affiliation

    Structural and Computational Biology Unit, European Molecular Biology Laboratory, Heidelberg, Germany. jbriggs@mrc-lmb.cam.ac.uk.



Macromolecules
Find similar proteins by:  (by identity cutoff)  |  Structure
Entity ID: 1
MoleculeChainsSequence LengthOrganismDetailsImage
Matrix protein 1A260Influenza A virus (A/Puerto Rico/8/1934(H1N1))Mutation(s): 1 
Gene Names: M
Find proteins for P03485 (Influenza A virus (strain A/Puerto Rico/8/1934 H1N1))
Explore P03485 
Go to UniProtKB:  P03485
Protein Feature View
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.80 Å
  • Aggregation State: HELICAL ARRAY 
  • Reconstruction Method: HELICAL 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Medical Research Council (MRC, United Kingdom)United KingdomMC_UP_1201/16
European Research Council (ERC)European UnionERC-CoG-648432
German Research Foundation (DFG)Germany240245660 - SFB1129

Revision History 

  • Version 1.0: 2020-10-14
    Type: Initial release
  • Version 1.1: 2020-10-21
    Changes: Structure summary