2VRS

Structure of avian reovirus sigmaC117-326, C2 crystal form

Summary for 2VRS

• Entry DOI: 10.2210/pdb2vrs/pdb
• Related: 2BSF 2JJL
• Descriptor: SIGMA-C CAPSID PROTEIN, GLYCEROL, ZINC ION, ... (6 entities in total)
• Functional Keywords: alpha-helical coiled coil, receptor-binding, triple beta-spiral, viral protein, virion, coiled coil, beta-barrel
• Biological source: AVIAN REOVIRUS
• Cellular location: Virion : Q992I2
• Total number of polymer chains: 3
• Total formula weight: 68662.18

Authors

Guardado-Calvo, P.,Fox, G.C.,Llamas-Saiz, A.L.,Benavente, J.,van Raaij, M.J. (deposition date: 2008-04-14, release date: 2009-01-13, Last modification date: 2023-12-13)

Primary citation

Guardado-Calvo, P.,Fox, G.C.,Llamas-Saiz, A.L.,van Raaij, M.J.
Crystallographic structure of the alpha-helical triple coiled-coil domain of avian reovirus S1133 fibre.
J. Gen. Virol., 90:672-677, 2009

PubMed Abstract: Avian reovirus fibre, a homo-trimer of the sigmaC protein, is a minor component of the avian reovirus outer capsid. It is anchored via a short N-terminal sequence to the inner capsid lambdaC 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 sigmaC 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 A (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.

PubMed: 19218213
DOI: 10.1099/vir.0.008276-0

Experimental method

X-RAY DIFFRACTION (1.75 Å)