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PDBsum entry 2vrs
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Viral protein
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PDB id
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2vrs
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References listed in PDB file
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Key reference
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Title
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Crystallographic structure of the alpha-Helical triple coiled-Coil domain of avian reovirus s1133 fibre.
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Authors
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P.Guardado-Calvo,
G.C.Fox,
A.L.Llamas-Saiz,
M.J.Van raaij.
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Ref.
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J Gen Virol, 2009,
90,
672-677.
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PubMed id
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Abstract
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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.
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Secondary reference #1
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Title
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Crystallization of the c-Terminal globular domain of avian reovirus fibre.
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Authors
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M.J.Van raaij,
X.L.Hermo parrado,
P.Guardado calvo,
G.C.Fox,
A.L.Llamas-Saiz,
C.Costas,
J.Martínez-Costas,
J.Benavente.
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Ref.
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Acta Crystallograph Sect F Struct Biol Cryst Commun, 2005,
61,
651-654.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1 Crystals of the avian reovirus fibre C-terminal
globular domain. (a) Irregular prisms belonging to space group
P6[3]22. (b) Bar-shaped crystals of space group P321 grown in
the presence of zinc sulfate. (c) Bar-shaped crystals of space
group P321 grown in the presence of cadmium sulfate. The
crystals are up to 0.15 mm wide (a), 0.1 mm long (b) and 0.4
mm long (c), respectively.
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The above figure is
reproduced from the cited reference
which is an Open Access publication published by the IUCr
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Secondary reference #2
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Title
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Structure of the carboxy-Terminal receptor-Binding domain of avian reovirus fibre sigmac.
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Authors
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P.Guardado calvo,
G.C.Fox,
X.L.Hermo parrado,
A.L.Llamas-Saiz,
C.Costas,
J.Martínez-Costas,
J.Benavente,
M.J.Van raaij.
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Ref.
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J Mol Biol, 2005,
354,
137-149.
[DOI no: ]
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PubMed id
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Figure 2.
Figure 2. Crystal structure of avian reovirus sigmaCD1-150.
(a) Stereo view of C^a atoms connected by lines. The three
monomers are coloured red, green and blue, and every tenth
residue of the red monomer is numbered. (b) Ribbon diagram in
the same orientation and colouring scheme as in (a). In the red
monomer, secondary structure elements are identified with upper
case letters for beta-strands and lower case letters for
helices. (c) The first triple beta-spiral repeat consisting of
amino acid residues 160-171 in ball-and-stick representation
covered by the final 2F[o] -F[c] electron density map contoured
at a s level of 1.0. (d) Top view of the sigmaC trimer.
Inter-monomer salt bridges are shown. Monomer backbones are
coloured yellow, orange and green. Figure 2, Figure 4 and Figure
5 were prepared using Bobscript,50 a modified version of
MOLSCRIPT.51
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Figure 4.
Figure 4. Mapping of conserved residues onto the structure
of sigmaC. (a) and (b) The structure of residues 160-326 of
crystal form IIz are shown in space-filled representation and
the locations of solvent-accessible residues (as judged by the
program SURFACE40) conserved in all known avian orthoreovirus
strains are indicated. The view in (b) is rotated 60° around
the vertical trimer axis as compared to (a). (c) Conserved amino
acid residues in the trimer interface. Monomer A is shown as a
coil, B and C in space-filled representation. The view is the
same as in (a). The locations of residues conserved in all known
avian orthoreovirus strains contacting another monomer are
indicated (contact less than 4 Å as calculated by the
program CONTACT40). The location of Asp277 is also shown,
although in some avian reovirus strains it is replaced by a Glu,
presumably still able to form a salt-bridge with Arg321.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Author's comment:
Structure of the receptor-binding domain of the avian reovirus fibre (protein sigmaC). Part of the shaft domain is also included, revealing two triple beta-spiral repeats. Future research will hopefully identify the avian receptor for this virus and show how it binds to sigmaC.
Mark J. van Raaij
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