Journal
JOURNAL OF GENERAL VIROLOGY
Volume 90, Issue -, Pages 672-677Publisher
MICROBIOLOGY SOC
DOI: 10.1099/vir.0.008276-0
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Funding
- Spanish Ministry of Education and Science [BFU2005-02974, BFU2005-24982-E]
- European Commission [ERAS-CT-2003-980409]
- BeNatural coordinated project [NMP4-CT-2006-033256]
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Avian reovirus fibre, a homo-trimer of the sigma 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 lambda 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 beta-spiral and 196-326 a beta-barrel head domain. Here we have expressed, purified and crystallized a major sigma 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 angstrom (0.175 nm) resolution, reveals an alpha-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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