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PDBsum entry 2jhc
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Viral protein
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PDB id
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2jhc
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Contents |
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* Residue conservation analysis
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DOI no:
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Nat Struct Biol
14:449-451
(2007)
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PubMed id:
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Bluetongue virus VP4 is an RNA-capping assembly line.
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G.Sutton,
J.M.Grimes,
D.I.Stuart,
P.Roy.
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ABSTRACT
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Eukaryotic organisms cap the 5' ends of their messenger RNAs by a series of four
chemical reactions. Some viruses achieve this using a single molecule; the
crystal structure of such an enzyme from bluetongue virus reveals an elongated
modular architecture that provides a scaffold for an assemblage of active sites,
two contributed by a domain of novel structure.
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Selected figure(s)
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Figure 1.
(a) Reaction mechanism for a type 1 cap. (b) VP4 domain
organization (domain names defined in text). Poorly ordered
loops are gray. Contact areas between domains are indicated. (c)
VP4 colored by domain, with active sites and ligands colored as
in a; view rotated 120° from b. AdoHcy in N7MTase and
2'OMTase are azure and orange, respectively. Cap analog is
yellow. (d) Active sites mapped onto electrostatic surface
representation of VP4 (colored as in c), and VP4 within BTV core.
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Figure 2.
(a) Left, 2'OMT domain colored from blue (N terminus) to red
(C terminus). Poorly ordered loop is gray. AdoHcy (magenta) and
G5'ppp5'G (blue) substrates are shown. Right, 2'OMTase active
sites of VP4 (purple) and VP39 (cyan). Carbon atoms and bonds of
significant residues are colored gray. VP4 ligands colored as at
left; VP39 AdoHcy and m^7G5'ppp5'G are marine and orange,
respectively. Red and yellow spheres represent cap analog 2'-O
and AdoHcy sulfur, respectively. (b) N7MT domain and AdoHcy, as
in a. Right, stereo view of N7MTase active sites of VP4 and
Ecm1. Carbon atoms and bonds of VP4 are gray, with guanine bases
purple and AdoHcy pink. Ecm1 is in olive, with cap analog orange
(blue sphere, N7) and AdoHcy lime (yellow spheres, sulfurs).
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2007,
14,
449-451)
copyright 2007.
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Figures were
selected
by an automated process.
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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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G.N.Murshudov,
P.Skubák,
A.A.Lebedev,
N.S.Pannu,
R.A.Steiner,
R.A.Nicholls,
M.D.Winn,
F.Long,
and
A.A.Vagin
(2011).
REFMAC5 for the refinement of macromolecular crystal structures.
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Acta Crystallogr D Biol Crystallogr,
67,
355-367.
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X.Zhang,
M.Boyce,
B.Bhattacharya,
X.Zhang,
S.Schein,
P.Roy,
and
Z.H.Zhou
(2010).
Bluetongue virus coat protein VP2 contains sialic acid-binding domains, and VP5 resembles enveloped virus fusion proteins.
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Proc Natl Acad Sci U S A,
107,
6292-6297.
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PDB code:
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E.Matsuo,
and
P.Roy
(2009).
Bluetongue virus VP6 acts early in the replication cycle and can form the basis of chimeric virus formation.
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J Virol,
83,
8842-8848.
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H.Dong,
S.Ren,
B.Zhang,
Y.Zhou,
F.Puig-Basagoiti,
H.Li,
and
P.Y.Shi
(2008).
West Nile virus methyltransferase catalyzes two methylations of the viral RNA cap through a substrate-repositioning mechanism.
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J Virol,
82,
4295-4307.
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H.Kroschewski,
S.P.Lim,
R.E.Butcher,
T.L.Yap,
J.Lescar,
P.J.Wright,
S.G.Vasudevan,
and
A.D.Davidson
(2008).
Mutagenesis of the dengue virus type 2 NS5 methyltransferase domain.
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J Biol Chem,
283,
19410-19421.
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I.Schwartz-Cornil,
P.P.Mertens,
V.Contreras,
B.Hemati,
F.Pascale,
E.Bréard,
P.S.Mellor,
N.J.MacLachlan,
and
S.Zientara
(2008).
Bluetongue virus: virology, pathogenesis and immunity.
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Vet Res,
39,
46.
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P.Roy
(2008).
Functional mapping of bluetongue virus proteins and their interactions with host proteins during virus replication.
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Cell Biochem Biophys,
50,
143-157.
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P.Roy
(2008).
Bluetongue virus: dissection of the polymerase complex.
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J Gen Virol,
89,
1789-1804.
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M.De la Peña,
O.J.Kyrieleis,
and
S.Cusack
(2007).
Structural insights into the mechanism and evolution of the vaccinia virus mRNA cap N7 methyl-transferase.
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EMBO J,
26,
4913-4925.
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PDB code:
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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
code is
shown on the right.
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