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Crystallographic structure of the -helical triple coiled-coil domain of avian reovirus S1133 fibre

¹ Departamento de Bioquímica e Bioloxía Molecular, Facultade de Farmacia, Universidade de Santiago de Compostela, E-15782 Santiago de Compostela, Spain
² Spanish CRG beamline BM16, European Synchrotron Radiation Facility, 6 rue Jules Horowitz, F-38043 Grenoble, France
³ Unidade de Raios X, Laboratorio Integral de Dinámica e Estructura de Biomoléculas José R. Carracido, Edificio CACTUS, Campus Sur, Universidade de Santiago de Compostela, E-15782 Santiago de Compostela, Spain
⁴ Instituto de Biología Molecular de Barcelona-CSIC, c/Josep-Samitier 1-5, E-08028 Barcelona, Spain

Correspondence
Mark J. van Raaij
mark.vanraaij{at}usc.es

Avian reovirus fibre, a homo-trimer of the C protein, is a minor component of the avian reovirus outer capsid. It is anchored via a short N-terminal sequence to the inner capsid C 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 C 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 -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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