5M1M

Crystal structure of matrix protein 1 from Influenza C virus (strain C/Ann Arbor/1/1950)

Summary for 5M1M

• Entry DOI: 10.2210/pdb5m1m/pdb
• Descriptor: Matrix protein 1, MAGNESIUM ION (3 entities in total)
• Functional Keywords: influenza c, matrix protein 1, viral protein
• Biological source: Influenza C virus (strain C/Ann Arbor/1/1950)
• Cellular location: Polyprotein p42: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Protein M1': Virion membrane ; Single-pass type II membrane protein . Protein CM2: Virion membrane ; Single-pass type I membrane protein : Q6I7B9
• Total number of polymer chains: 1
• Total formula weight: 17526.09

Authors

Radzimanowski, J.,Weissenhorn, W. (deposition date: 2016-10-09, release date: 2017-02-08, Last modification date: 2024-05-08)

Primary citation

Saletti, D.,Radzimanowski, J.,Effantin, G.,Midtvedt, D.,Mangenot, S.,Weissenhorn, W.,Bassereau, P.,Bally, M.
The Matrix protein M1 from influenza C virus induces tubular membrane invaginations in an in vitro cell membrane model.
Sci Rep, 7:40801-40801, 2017

PubMed Abstract: Matrix proteins from enveloped viruses play an important role in budding and stabilizing virus particles. In order to assess the role of the matrix protein M1 from influenza C virus (M1-C) in plasma membrane deformation, we have combined structural and in vitro reconstitution experiments with model membranes. We present the crystal structure of the N-terminal domain of M1-C and show by Small Angle X-Ray Scattering analysis that full-length M1-C folds into an elongated structure that associates laterally into ring-like or filamentous polymers. Using negatively charged giant unilamellar vesicles (GUVs), we demonstrate that M1-C full-length binds to and induces inward budding of membrane tubules with diameters that resemble the diameter of viruses. Membrane tubule formation requires the C-terminal domain of M1-C, corroborating its essential role for M1-C polymerization. Our results indicate that M1-C assembly on membranes constitutes the driving force for budding and suggest that M1-C plays a key role in facilitating viral egress.

PubMed: 28120862
DOI: 10.1038/srep40801

Experimental method

X-RAY DIFFRACTION (1.5 Å)