Download MendeleyStructure and self-assembly of the calcium binding matrix protein of human metapneumovirus.
Leyrat, C., Renner, M., Harlos, K., Huiskonen, J.T., Grimes, J.M.(2014) Structure 22: 136-148
- PubMed: 24316400
- DOI: https://doi.org/10.1016/j.str.2013.10.013
- Primary Citation of Related Structures:
4LP7 - PubMed Abstract:
The matrix protein (M) of paramyxoviruses plays a key role in determining virion morphology by directing viral assembly and budding. Here, we report the crystal structure of the human metapneumovirus M at 2.8 Å resolution in its native dimeric state. The structure reveals the presence of a high-affinity Ca²⁺ binding site. Molecular dynamics simulations (MDS) predict a secondary lower-affinity site that correlates well with data from fluorescence-based thermal shift assays. By combining small-angle X-ray scattering with MDS and ensemble analysis, we captured the structure and dynamics of M in solution. Our analysis reveals a large positively charged patch on the protein surface that is involved in membrane interaction. Structural analysis of DOPC-induced polymerization of M into helical filaments using electron microscopy leads to a model of M self-assembly. The conservation of the Ca²⁺ binding sites suggests a role for calcium in the replication and morphogenesis of pneumoviruses.
Organizational Affiliation:
Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK.
