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-Structure paper
タイトル | Structure and self-assembly of the calcium binding matrix protein of human metapneumovirus. |
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ジャーナル・号・ページ | Structure, Vol. 22, Issue 1, Page 136-148, Year 2014 |
掲載日 | 2014年1月7日 |
著者 | Cedric Leyrat / Max Renner / Karl Harlos / Juha T Huiskonen / Jonathan M Grimes / |
PubMed 要旨 | 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 ...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. |
リンク | Structure / PubMed:24316400 / PubMed Central |
手法 | EM (らせん対称) / X線回折 |
解像度 | 2.83 - 28.0 Å |
構造データ | EMDB-2415: PDB-4lp7: |
化合物 | ChemComp-CA: ChemComp-CL: ChemComp-HOH: |
由来 |
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キーワード | CALCIUM BINDING PROTEIN / twisted beta sandwich / viral matrix / lipid binding |