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Avian reovirus fibre, a homo-trimer of the σC protein, is a minor component of the avian reovirus outer capsid. It is anchored via a short N-terminal sequence to the inner capsid λC pentamer, and its protruding globular C-terminal domain is responsible for primary host cell attachment. We have previously solved the structure of a receptor-binding fragment in which residues 160–191 form a triple β-spiral and 196–326 a β-barrel head domain. Here we have expressed, purified and crystallized a major σC fragment comprising residues 117–326. Its structure, which was solved by molecular replacement using the previously determined receptor-binding domain structure and refined to 1.75 Å (0.175 nm) resolution, reveals an α-helical triple coiled-coil connected to the previously solved structure by a zinc-ion-containing linker. The coiled-coil domain contains two chloride ion binding sites, as well as specific trimerization and registration sequences. The linker may act as a functionally important hinge.
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