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Contents |
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1284 a.a.
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1031 a.a.
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1221 a.a.
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417 a.a.
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* Residue conservation analysis
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PDB id:
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| Name: |
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Virus
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Title:
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Reovirus core
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Structure:
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Lambda2. Chain: a. Lambda1. Chain: b, c. Sigma2. Chain: d, e
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Source:
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Reovirus sp.. Organism_taxid: 10891. Strain: reassortant f18. Strain: reassortant f18
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Resolution:
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3.60Å
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R-factor:
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0.206
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R-free:
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0.208
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Authors:
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K.M.Reinisch,M.L.Nibert,S.C.Harrison
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Key ref:
|
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K.M.Reinisch
et al.
(2000).
Structure of the reovirus core at 3.6 A resolution.
Nature,
404,
960-967.
PubMed id:
DOI:
|
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Date:
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29-Feb-00
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Release date:
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12-Jul-00
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PROCHECK
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Headers
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References
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P11079
(LMBD2_REOVD) -
Outer capsid protein lambda-2 from Reovirus type 3 (strain Dearing)
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Seq: Struc:
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1289 a.a.
1284 a.a.
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P15024
(LMBD1_REOVD) -
Inner capsid protein lambda-1 from Reovirus type 3 (strain Dearing)
|
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Seq: Struc:
|
 |
 |
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1275 a.a.
1031 a.a.*
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Enzyme class 1:
|
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Chain A:
E.C.2.1.1.56
- mRNA (guanine-N(7))-methyltransferase.
|
|
 |
 |
 |
 |
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Reaction:
|
 |
a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L- methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
|
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5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA
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+
|
S-adenosyl-L- methionine
|
=
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5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA
|
+
|
S-adenosyl-L-homocysteine
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 |
 |
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 |
 |
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Enzyme class 2:
|
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Chain A:
E.C.2.7.7.50
- mRNA guanylyltransferase.
|
|
 |
 |
 |
 |
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Reaction:
|
 |
a 5'-end diphospho-ribonucleoside in mRNA + GTP + H+ = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate
|
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 |
 |
 |
 |
5'-end diphospho-ribonucleoside in mRNA
|
+
|
GTP
|
+
|
H(+)
|
=
|
5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA
|
+
|
diphosphate
|
|
 |
 |
 |
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 |
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 |
 |
Enzyme class 3:
|
 |
Chains B, C:
E.C.3.6.4.13
- Rna helicase.
|
|
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 |
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 |
 |
Reaction:
|
 |
ATP + H2O = ADP + phosphate + H+
|
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 |
 |
 |
 |
ATP
|
+
|
H2O
|
=
|
ADP
|
+
|
phosphate
|
+
|
H(+)
|
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 |
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 |
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 |
 |
 |
|
Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
|
|
 |
|
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
|
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| |
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| |
|
DOI no:
|
Nature
404:960-967
(2000)
|
|
PubMed id:
|
|
|
|
|
| |
|
Structure of the reovirus core at 3.6 A resolution.
|
|
K.M.Reinisch,
M.L.Nibert,
S.C.Harrison.
|
|
|
|
| |
ABSTRACT
|
|
|
| |
|
The reovirus core is an assembly with a relative molecular mass of 52 million
that synthesizes, modifies and exports viral messenger RNA. Analysis of its
structure by X-ray crystallography shows that there are alternative, specific
and completely non-equivalent contacts made by several surfaces of two of its
proteins; that the RNA capping and export apparatus is a hollow cylinder, which
probably sequesters its substrate to ensure completion of the capping reactions;
that the genomic double-stranded RNA is coiled into concentric layers within the
particle; and that there is a protein shell that appears to be common to all
groups of double-stranded RNA viruses.
|
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| |
Selected figure(s)
|
|
|
| |
 |
 |
|
 |
|
 |
Figure 1.
Figure 1: The reovirus core particle, represented by C
alpha- traces
of the constituent subunits. lambda- 1
(relative molecular mass (M[r]) 142K (ref.46), 120 copies; shown
in red) forms the shell that packages RNA and defines the
symmetry and size of the particle. 2
(M[r] 47K, 150 copies; shown as yellow, green and white nodules)
stabilizes the 1
shell. 2
(M[ r] 144K, 60 copies; shown in blue) forms turret-like
structures around the fivefold axes that cap the nascent mRNA
and organize its extrusion.
|
 |
Figure 6.
Figure 6: The capping complex. a, b, 2
turret (about 120 Å diameter and 80 Å tall) viewed from the top
and side, respectively. The five elongated 2
monomers, each shown in a different colour, wrap around the
outer surface, with their long axes at about 45° to the radial
direction. c, The 2
monomer, viewed from the inside of the pentamer (the blue
monomer in b). The GTase domain is red, methylase-1 is yellow,
methylase-2 is green and the immunoglobulin-like domains are
blue. Red SAH molecules mark the SAM-binding sites. d, GTase
domain at 90° to c, in graded colours with the N terminus red
and the C terminus blue. Side chains of K190 and K171 are shown.
e, Diagrams of SAM-binding domains. The 'universal' SAM-binding
domain is shown in black19, 20; methylase-1 is yellow and
methylase-2 is green. Secondary structural elements are aligned
vertically with their equivalents in the universal fold. The
SAM-binding position with respect to the -sheet
is labelled. f, Two monomers of 2
(labelled A and B) with the immunoglobulin-like domains detached
and viewed from the interior of the turret. Monomer A includes
GTase 'a' and methylases 'a1' and 'a2'; B includes 'b', 'b1' and
'b2'. Coloured as in c. Red SAH molecules indicate SAM-binding
locations. Blue arrows indicate the GTase active site. g, SAH
density for methylase-1 in a 4 Å, 2F[o]- F[c] map made with data
from crystals soaked in 2 mM SAH. SAH binding is accompanied by
conformational changes in residues 519-524 and 579-587. Some
residues that may interact with SAH are labelled. h, SAH density
for methylase-2.
|
 |
|
|
|
| |
The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2000,
404,
960-967)
copyright 2000.
|
|
| |
Figures were
selected
by the author.
|
|
|
|
|
 |
 |
|
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 |
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 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
 |
| |
PubMed id
|
 |
Reference
|
 |
|
|
|
 |
E.Decroly,
F.Ferron,
J.Lescar,
and
B.Canard
(2012).
Conventional and unconventional mechanisms for capping viral mRNA.
|
| |
Nat Rev Microbiol,
10,
51-65.
|
 |
|
|
|
|
 |
S.D.Trask,
S.M.McDonald,
and
J.T.Patton
(2012).
Structural insights into the coupling of virion assembly and rotavirus replication.
|
| |
Nat Rev Microbiol,
10,
165-177.
|
 |
|
|
|
|
 |
L.Cheng,
J.Sun,
K.Zhang,
Z.Mou,
X.Huang,
G.Ji,
F.Sun,
J.Zhang,
and
P.Zhu
(2011).
Atomic model of a cypovirus built from cryo-EM structure provides insight into the mechanism of mRNA capping.
|
| |
Proc Natl Acad Sci U S A,
108,
1373-1378.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
N.Grigorieff,
and
S.C.Harrison
(2011).
Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy.
|
| |
Curr Opin Struct Biol,
21,
265-273.
|
 |
|
|
|
|
 |
B.McClain,
E.Settembre,
B.R.Temple,
A.R.Bellamy,
and
S.C.Harrison
(2010).
X-ray crystal structure of the rotavirus inner capsid particle at 3.8 A resolution.
|
| |
J Mol Biol,
397,
587-599.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
C.L.Lawson
(2010).
Unified data resource for cryo-EM.
|
| |
Methods Enzymol,
483,
73-90.
|
 |
|
|
|
|
 |
D.Luque,
J.M.González,
D.Garriga,
S.A.Ghabrial,
W.M.Havens,
B.Trus,
N.Verdaguer,
J.L.Carrascosa,
and
J.R.Castón
(2010).
The T=1 capsid protein of Penicillium chrysogenum virus is formed by a repeated helix-rich core indicative of gene duplication.
|
| |
J Virol,
84,
7256-7266.
|
 |
|
|
|
|
 |
J.A.den Boon,
A.Diaz,
and
P.Ahlquist
(2010).
Cytoplasmic viral replication complexes.
|
| |
Cell Host Microbe,
8,
77-85.
|
 |
|
|
|
|
 |
J.Zhu,
L.Cheng,
Q.Fang,
Z.H.Zhou,
and
B.Honig
(2010).
Building and refining protein models within cryo-electron microscopy density maps based on homology modeling and multiscale structure refinement.
|
| |
J Mol Biol,
397,
835-851.
|
 |
|
|
|
|
 |
L.Cheng,
J.Zhu,
W.H.Hui,
X.Zhang,
B.Honig,
Q.Fang,
and
Z.H.Zhou
(2010).
Backbone model of an aquareovirus virion by cryo-electron microscopy and bioinformatics.
|
| |
J Mol Biol,
397,
852-863.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
L.J.Yap,
D.Luo,
K.Y.Chung,
S.P.Lim,
C.Bodenreider,
C.Noble,
P.Y.Shi,
and
J.Lescar
(2010).
Crystal structure of the dengue virus methyltransferase bound to a 5'-capped octameric RNA.
|
| |
PLoS One,
5,
0.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
M.Bouvet,
C.Debarnot,
I.Imbert,
B.Selisko,
E.J.Snijder,
B.Canard,
and
E.Decroly
(2010).
In vitro reconstitution of SARS-coronavirus mRNA cap methylation.
|
| |
PLoS Pathog,
6,
e1000863.
|
 |
|
|
|
|
 |
N.Miyazaki,
B.Wu,
K.Hagiwara,
C.Y.Wang,
L.Xing,
L.Hammar,
A.Higashiura,
T.Tsukihara,
A.Nakagawa,
T.Omura,
and
R.H.Cheng
(2010).
The functional organization of the internal components of Rice dwarf virus.
|
| |
J Biochem,
147,
843-850.
|
 |
|
|
|
|
 |
Y.J.Tao,
and
Q.Ye
(2010).
RNA virus replication complexes.
|
| |
PLoS Pathog,
6,
e1000943.
|
 |
|
|
|
|
 |
Z.Dauter,
M.Jaskolski,
and
A.Wlodawer
(2010).
Impact of synchrotron radiation on macromolecular crystallography: a personal view.
|
| |
J Synchrotron Radiat,
17,
433-444.
|
 |
|
|
|
|
 |
A.A.Demidenko,
and
M.L.Nibert
(2009).
Probing the transcription mechanisms of reovirus cores with molecules that alter RNA duplex stability.
|
| |
J Virol,
83,
5659-5670.
|
 |
|
|
|
|
 |
A.Korkut,
and
W.A.Hendrickson
(2009).
A force field for virtual atom molecular mechanics of proteins.
|
| |
Proc Natl Acad Sci U S A,
106,
15667-15672.
|
 |
|
|
|
|
 |
B.Sherry
(2009).
Rotavirus and reovirus modulation of the interferon response.
|
| |
J Interferon Cytokine Res,
29,
559-567.
|
 |
|
|
|
|
 |
E.B.Ludmir,
and
L.W.Enquist
(2009).
Viral genomes are part of the phylogenetic tree of life.
|
| |
Nat Rev Microbiol,
7,
615; author reply 615.
|
 |
|
|
|
|
 |
G.R.Nemerow,
L.Pache,
V.Reddy,
and
P.L.Stewart
(2009).
Insights into adenovirus host cell interactions from structural studies.
|
| |
Virology,
384,
380-388.
|
 |
|
|
|
|
 |
J.Pan,
L.Dong,
L.Lin,
W.F.Ochoa,
R.S.Sinkovits,
W.M.Havens,
M.L.Nibert,
T.S.Baker,
S.A.Ghabrial,
and
Y.J.Tao
(2009).
Atomic structure reveals the unique capsid organization of a dsRNA virus.
|
| |
Proc Natl Acad Sci U S A,
106,
4225-4230.
|
 |
|
PDB codes:
|
 |
|
|
|
|
|
 |
L.Zhang,
M.A.Agosto,
T.Ivanovic,
D.S.King,
M.L.Nibert,
and
S.C.Harrison
(2009).
Requirements for the formation of membrane pores by the reovirus myristoylated micro1N peptide.
|
| |
J Virol,
83,
7004-7014.
|
 |
|
|
|
|
 |
M.Jalasvuori,
S.T.Jaatinen,
S.Laurinavicius,
E.Ahola-Iivarinen,
N.Kalkkinen,
D.H.Bamford,
and
J.K.Bamford
(2009).
The closest relatives of icosahedral viruses of thermophilic bacteria are among viruses and plasmids of the halophilic archaea.
|
| |
J Virol,
83,
9388-9397.
|
 |
|
|
|
|
 |
S.Duquerroy,
B.Da Costa,
C.Henry,
A.Vigouroux,
S.Libersou,
J.Lepault,
J.Navaza,
B.Delmas,
and
F.A.Rey
(2009).
The picobirnavirus crystal structure provides functional insights into virion assembly and cell entry.
|
| |
EMBO J,
28,
1655-1665.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
Z.Li,
M.L.Baker,
W.Jiang,
M.K.Estes,
and
B.V.Prasad
(2009).
Rotavirus architecture at subnanometer resolution.
|
| |
J Virol,
83,
1754-1766.
|
 |
|
|
|
|
 |
E.Decroly,
I.Imbert,
B.Coutard,
M.Bouvet,
B.Selisko,
K.Alvarez,
A.E.Gorbalenya,
E.J.Snijder,
and
B.Canard
(2008).
Coronavirus nonstructural protein 16 is a cap-0 binding enzyme possessing (nucleoside-2'O)-methyltransferase activity.
|
| |
J Virol,
82,
8071-8084.
|
 |
|
|
|
|
 |
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.
|
| |
J Virol,
82,
4295-4307.
|
 |
|
|
|
|
 |
H.Dong,
S.Ren,
H.Li,
and
P.Y.Shi
(2008).
Separate molecules of West Nile virus methyltransferase can independently catalyze the N7 and 2'-O methylations of viral RNA cap.
|
| |
Virology,
377,
1-6.
|
 |
|
|
|
|
 |
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.
|
| |
J Biol Chem,
283,
19410-19421.
|
 |
|
|
|
|
 |
I.I.Mendez,
S.G.Weiner,
Y.M.She,
M.Yeager,
and
K.M.Coombs
(2008).
Conformational changes accompany activation of reovirus RNA-dependent RNA transcription.
|
| |
J Struct Biol,
162,
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|
 |
|
|
|
|
 |
J.Tang,
W.F.Ochoa,
R.S.Sinkovits,
B.T.Poulos,
S.A.Ghabrial,
D.V.Lightner,
T.S.Baker,
and
M.L.Nibert
(2008).
Infectious myonecrosis virus has a totivirus-like, 120-subunit capsid, but with fiber complexes at the fivefold axes.
|
| |
Proc Natl Acad Sci U S A,
105,
17526-17531.
|
 |
|
|
|
|
 |
L.Cheng,
Q.Fang,
S.Shah,
I.C.Atanasov,
and
Z.H.Zhou
(2008).
Subnanometer-resolution structures of the grass carp reovirus core and virion.
|
| |
J Mol Biol,
382,
213-222.
|
 |
|
|
|
|
 |
N.Miyazaki,
T.Uehara-Ichiki,
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T.Omura,
and
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(2008).
Structural evolution of reoviridae revealed by oryzavirus in acquiring the second capsid shell.
|
| |
J Virol,
82,
11344-11353.
|
 |
|
|
|
|
 |
P.Guardado-Calvo,
L.Vazquez-Iglesias,
J.Martinez-Costas,
A.L.Llamas-Saiz,
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X.L.Hermo-Parrado,
J.Benavente,
and
M.J.van Raaij
(2008).
Crystal structure of the avian reovirus inner capsid protein sigmaA.
|
| |
J Virol,
82,
11208-11216.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
P.Roy
(2008).
Bluetongue virus: dissection of the polymerase complex.
|
| |
J Gen Virol,
89,
1789-1804.
|
 |
|
|
|
|
 |
S.Libersou,
X.Siebert,
M.Ouldali,
L.F.Estrozi,
J.Navaza,
A.Charpilienne,
P.Garnier,
D.Poncet,
and
J.Lepault
(2008).
Geometric mismatches within the concentric layers of rotavirus particles: a potential regulatory switch of viral particle transcription activity.
|
| |
J Virol,
82,
2844-2852.
|
 |
|
|
|
|
 |
S.M.McDonald,
and
J.T.Patton
(2008).
Molecular characterization of a subgroup specificity associated with the rotavirus inner capsid protein VP2.
|
| |
J Virol,
82,
2752-2764.
|
 |
|
|
|
|
 |
W.F.Ochoa,
W.M.Havens,
R.S.Sinkovits,
M.L.Nibert,
S.A.Ghabrial,
and
T.S.Baker
(2008).
Partitivirus structure reveals a 120-subunit, helix-rich capsid with distinctive surface arches formed by quasisymmetric coat-protein dimers.
|
| |
Structure,
16,
776-786.
|
 |
|
|
|
|
 |
X.Yu,
L.Jin,
and
Z.H.Zhou
(2008).
3.88 A structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy.
|
| |
Nature,
453,
415-419.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
Z.H.Zhou
(2008).
Towards atomic resolution structural determination by single-particle cryo-electron microscopy.
|
| |
Curr Opin Struct Biol,
18,
218-228.
|
 |
|
|
|
|
 |
B.G.Kopek,
G.Perkins,
D.J.Miller,
M.H.Ellisman,
and
P.Ahlquist
(2007).
Three-dimensional analysis of a viral RNA replication complex reveals a virus-induced mini-organelle.
|
| |
PLoS Biol,
5,
e220.
|
 |
|
|
|
|
 |
E.Mastrangelo,
M.Bollati,
M.Milani,
B.Selisko,
F.Peyrane,
B.Canard,
G.Grard,
X.de Lamballerie,
and
M.Bolognesi
(2007).
Structural bases for substrate recognition and activity in Meaban virus nucleoside-2'-O-methyltransferase.
|
| |
Protein Sci,
16,
1133-1145.
|
 |
|
PDB code:
|
 |
|
|
|
|
|
 |
G.Sutton,
J.M.Grimes,
D.I.Stuart,
and
P.Roy
(2007).
Bluetongue virus VP4 is an RNA-capping assembly line.
|
| |
Nat Struct Mol Biol,
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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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