RT Journal Article SR Electronic(1) A1 Guardado-Calvo, Pablo A1 Fox, Gavin C. A1 Llamas-Saiz, Antonio L. A1 van Raaij, Mark J.YR 2009 T1 Crystallographic structure of the α-helical triple coiled-coil domain of avian reovirus S1133 fibre JF Journal of General Virology, VO 90 IS 3 SP 672 OP 677 DO https://doi.org/10.1099/vir.0.008276-0 PB Microbiology Society, SN 1465-2099, AB 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., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.008276-0