4LP7
Crystal structure of the human metapneumovirus matrix protein
Summary for 4LP7
| Entry DOI | 10.2210/pdb4lp7/pdb |
| Descriptor | Matrix protein M, CALCIUM ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | twisted beta sandwich, viral matrix, lipid binding, calcium binding protein |
| Biological source | Human metapneumovirus |
| Total number of polymer chains | 4 |
| Total formula weight | 110876.50 |
| Authors | Leyrat, C.,Harlos, K.,Grimes, J.M. (deposition date: 2013-07-15, release date: 2013-12-18, Last modification date: 2023-09-20) |
| Primary citation | Leyrat, C.,Renner, M.,Harlos, K.,Huiskonen, J.T.,Grimes, J.M. Structure and self-assembly of the calcium binding matrix protein of human metapneumovirus. Structure, 22:136-148, 2014 Cited by 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. PubMed: 24316400DOI: 10.1016/j.str.2013.10.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.83 Å) |
Structure validation
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