4lp7 | pdb_00004lp7

Crystal structure of the human metapneumovirus matrix protein

spinqualitylabelsall models 4lp7, resolution 2.83Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4lp7 is a 4 chain structure with sequence from Hmpv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CL Gene: M (HMPV) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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 A 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. Structure and Self-Assembly of the Calcium Binding Matrix Protein of Human Metapneumovirus.,Leyrat C, Renner M, Harlos K, Huiskonen JT, Grimes JM Structure. 2013 Dec 3. pii: S0969-2126(13)00425-5. doi:, 10.1016/j.str.2013.10.013. PMID:24316400 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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