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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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Contents |
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* Residue conservation analysis
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PDB id:
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Viral protein
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Title:
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Structure of avian reovirus sigmac117-326, c2 crystal form
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Structure:
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Sigma-c capsid protein. Chain: a, b, c. Fragment: residues 117-326. Synonym: sigma-3 protein, sigma c. Engineered: yes
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Source:
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Avian reovirus. Organism_taxid: 38170. Strain: s1133. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_variant: de3. Other_details: the avian reovirus strain s1133 was originally provided by dr. Philip i.Marcus when dr. J.Benavente was a roche visiting scientist in the laboratory of dr. A.Shatkin
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Resolution:
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1.75Å
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R-factor:
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0.180
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R-free:
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0.218
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Authors:
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P.Guardado-Calvo,G.C.Fox,A.L.Llamas-Saiz,J.Benavente,M.J.Van Raaij
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Key ref:
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P.Guardado-Calvo
et al.
(2009).
Crystallographic structure of the alpha-helical triple coiled-coil domain of avian reovirus S1133 fibre.
J Gen Virol,
90,
672-677.
PubMed id:
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Date:
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14-Apr-08
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Release date:
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13-Jan-09
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PROCHECK
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Headers
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References
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Q992I2
(SIGC_ARVS1) -
Sigma-C capsid protein from Avian reovirus (strain S1133)
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Seq:
Struc:
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326 a.a.
205 a.a.
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Key: |
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Secondary structure |
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CATH domain |
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J Gen Virol
90:672-677
(2009)
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PubMed id:
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Crystallographic structure of the alpha-helical triple coiled-coil domain of avian reovirus S1133 fibre.
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P.Guardado-Calvo,
G.C.Fox,
A.L.Llamas-Saiz,
M.J.van Raaij.
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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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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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E.C.Schulz,
and
R.Ficner
(2011).
Knitting and snipping: chaperones in β-helix folding.
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Curr Opin Struct Biol,
21,
232-239.
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M.D.Hartmann,
O.Ridderbusch,
K.Zeth,
R.Albrecht,
O.Testa,
D.N.Woolfson,
G.Sauer,
S.Dunin-Horkawicz,
A.N.Lupas,
and
B.H.Alvarez
(2009).
A coiled-coil motif that sequesters ions to the hydrophobic core.
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Proc Natl Acad Sci U S A,
106,
16950-16955.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
