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PDBsum entry 2ms2
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* Residue conservation analysis
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J Mol Biol
234:620-639
(1993)
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PubMed id:
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The refined structure of bacteriophage MS2 at 2.8 A resolution.
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R.Golmohammadi,
K.Valegård,
K.Fridborg,
L.Liljas.
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ABSTRACT
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Bacteriophage MS2 is an icosahedral virus with 180 copies of a coat protein
forming a shell around a single-stranded RNA molecule. The coat protein subunits
form a lattice with the triangulation number T = 3. The coat protein has a fold
which is different from the fold of all other viral coat proteins so far known.
It consists of a five-stranded beta sheet facing the inside of the particle, and
a hairpin and two helices on the outside. The crystal structure has been refined
at 2.8 A resolution. The final R-factor was 0.189 for reflections with F > 2
sigma, and the root-mean-square deviation from idealized bond lengths and bond
angles was 0.015 A and 2.9 degrees, respectively. The three chemically identical
conformers A, B and C are largely similar. The B conformer has a unique
conformation in one loop, which is involved in 5-fold interactions, while the A
and C conformers, which are involved in the quasi-6-fold contacts, are similar
throughout the structure. One cis-proline has been identified in the B conformer
but the corresponding prolines in A and C are of the trans isomer. This residue
is conserved within small RNA coliphages and it is proposed that this
isomerization enables a less elongated loop (FG) around the 5-fold axis, thus
creating a channel. The extensive dimer contact supports the idea of dimers as
initial building blocks. An assembly pathway is proposed where five dimers
converge into a pentamer and 12 pentamers are linked together with free dimers
creating a complete particle.
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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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K.Toropova,
P.G.Stockley,
and
N.A.Ranson
(2011).
Visualising a viral RNA genome poised for release from its receptor complex.
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J Mol Biol,
408,
408-419.
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E.C.Dykeman,
and
R.Twarock
(2010).
All-atom normal-mode analysis reveals an RNA-induced allostery in a bacteriophage coat protein.
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Phys Rev E Stat Nonlin Soft Matter Phys,
81,
031908.
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K.J.Koudelka,
and
M.Manchester
(2010).
Chemically modified viruses: principles and applications.
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Curr Opin Chem Biol,
14,
810-817.
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T.W.Knapman,
V.L.Morton,
N.J.Stonehouse,
P.G.Stockley,
and
A.E.Ashcroft
(2010).
Determining the topology of virus assembly intermediates using ion mobility spectrometry-mass spectrometry.
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Rapid Commun Mass Spectrom,
24,
3033-3042.
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V.L.Morton,
W.Burkitt,
G.O'Connor,
N.J.Stonehouse,
P.G.Stockley,
and
A.E.Ashcroft
(2010).
RNA-induced conformational changes in a viral coat protein studied by hydrogen/deuterium exchange mass spectrometry.
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Phys Chem Chem Phys,
12,
13468-13475.
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E.Vo,
S.Rengasamy,
and
R.Shaffer
(2009).
Development of a test system to evaluate procedures for decontamination of respirators containing viral droplets.
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Appl Environ Microbiol,
75,
7303-7309.
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S.Katen,
and
A.Zlotnick
(2009).
The thermodynamics of virus capsid assembly.
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Methods Enzymol,
455,
395-417.
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T.Keef,
and
R.Twarock
(2009).
Affine extensions of the icosahedral group with applications to the three-dimensional organisation of simple viruses.
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J Math Biol,
59,
287-313.
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A.A.Akunyili,
M.Alfatlawi,
B.Upadhyaya,
L.S.Rhoads,
H.Eichelberger,
and
C.T.Van Bell
(2008).
Ingestion without inactivation of bacteriophages by Tetrahymena.
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J Eukaryot Microbiol,
55,
207-213.
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D.S.Peabody,
B.Manifold-Wheeler,
A.Medford,
S.K.Jordan,
J.do Carmo Caldeira,
and
B.Chackerian
(2008).
Immunogenic display of diverse peptides on virus-like particles of RNA phage MS2.
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J Mol Biol,
380,
252-263.
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J.Langlet,
F.Gaboriaud,
C.Gantzer,
and
J.F.Duval
(2008).
Impact of chemical and structural anisotropy on the electrophoretic mobility of spherical soft multilayer particles: the case of bacteriophage MS2.
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Biophys J,
94,
3293-3312.
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J.M.Hooker,
J.P.O'Neil,
D.W.Romanini,
S.E.Taylor,
and
M.B.Francis
(2008).
Genome-free viral capsids as carriers for positron emission tomography radiolabels.
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Mol Imaging Biol,
10,
182-191.
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P.Plevka,
K.Tars,
and
L.Liljas
(2008).
Crystal packing of a bacteriophage MS2 coat protein mutant corresponds to octahedral particles.
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Protein Sci,
17,
1731-1739.
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PDB code:
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V.L.Morton,
P.G.Stockley,
N.J.Stonehouse,
and
A.E.Ashcroft
(2008).
Insights into virus capsid assembly from non-covalent mass spectrometry.
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Mass Spectrom Rev,
27,
575-595.
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J.C.Caldeira,
and
D.S.Peabody
(2007).
Stability and assembly in vitro of bacteriophage PP7 virus-like particles.
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J Nanobiotechnology,
5,
10.
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J.Langlet,
F.Gaboriaud,
and
C.Gantzer
(2007).
Effects of pH on plaque forming unit counts and aggregation of MS2 bacteriophage.
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J Appl Microbiol,
103,
1632-1638.
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A.H.Andreotti
(2006).
Opening the pore hinges on proline.
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Nat Chem Biol,
2,
13-14.
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J.Simonet,
and
C.Gantzer
(2006).
Inactivation of poliovirus 1 and F-specific RNA phages and degradation of their genomes by UV irradiation at 254 nanometers.
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Appl Environ Microbiol,
72,
7671-7677.
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W.T.Horn,
K.Tars,
E.Grahn,
C.Helgstrand,
A.J.Baron,
H.Lago,
C.J.Adams,
D.S.Peabody,
S.E.Phillips,
N.J.Stonehouse,
L.Liljas,
and
P.G.Stockley
(2006).
Structural basis of RNA binding discrimination between bacteriophages Qbeta and MS2.
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Structure,
14,
487-495.
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PDB codes:
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C.J.Hogan,
E.M.Kettleson,
M.H.Lee,
B.Ramaswami,
L.T.Angenent,
and
P.Biswas
(2005).
Sampling methodologies and dosage assessment techniques for submicrometre and ultrafine virus aerosol particles.
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J Appl Microbiol,
99,
1422-1434.
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E.J.van Schaik,
C.L.Giltner,
G.F.Audette,
D.W.Keizer,
D.L.Bautista,
C.M.Slupsky,
B.D.Sykes,
and
R.T.Irvin
(2005).
DNA binding: a novel function of Pseudomonas aeruginosa type IV pili.
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J Bacteriol,
187,
1455-1464.
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A.Fokine,
P.R.Chipman,
P.G.Leiman,
V.V.Mesyanzhinov,
V.B.Rao,
and
M.G.Rossmann
(2004).
Molecular architecture of the prolate head of bacteriophage T4.
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Proc Natl Acad Sci U S A,
101,
6003-6008.
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S.M.Lima,
D.S.Peabody,
J.L.Silva,
and
A.C.de Oliveira
(2004).
Mutations in the hydrophobic core and in the protein-RNA interface affect the packing and stability of icosahedral viruses.
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Eur J Biochem,
271,
135-145.
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W.T.Horn,
M.A.Convery,
N.J.Stonehouse,
C.J.Adams,
L.Liljas,
S.E.Phillips,
and
P.G.Stockley
(2004).
The crystal structure of a high affinity RNA stem-loop complexed with the bacteriophage MS2 capsid: further challenges in the modeling of ligand-RNA interactions.
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RNA,
10,
1776-1782.
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PDB code:
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C.D.Anobom,
S.C.Albuquerque,
F.P.Albernaz,
A.C.Oliveira,
J.L.Silva,
D.S.Peabody,
A.P.Valente,
and
F.C.Almeida
(2003).
Structural studies of MS2 bacteriophage virus particle disassembly by nuclear magnetic resonance relaxation measurements.
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Biophys J,
84,
3894-3903.
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D.S.Peabody
(2003).
A Viral Platform for Chemical Modification and Multivalent Display.
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J Nanobiotechnology,
1,
5.
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D.S.Peabody,
and
L.Al-Bitar
(2001).
Isolation of viral coat protein mutants with altered assembly and aggregation properties.
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Nucleic Acids Res,
29,
E113.
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E.Grahn,
T.Moss,
C.Helgstrand,
K.Fridborg,
M.Sundaram,
K.Tars,
H.Lago,
N.J.Stonehouse,
D.R.Davis,
P.G.Stockley,
and
L.Liljas
(2001).
Structural basis of pyrimidine specificity in the MS2 RNA hairpin-coat-protein complex.
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RNA,
7,
1616-1627.
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PDB codes:
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R.Tuma,
H.Tsuruta,
J.M.Benevides,
P.E.Prevelige,
and
G.J.Thomas
(2001).
Characterization of subunit structural changes accompanying assembly of the bacteriophage P22 procapsid.
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Biochemistry,
40,
665-674.
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Y.S.Nam,
A.Petrovic,
K.S.Jeong,
and
S.Venkatesan
(2001).
Exchange of the basic domain of human immunodeficiency virus type 1 Rev for a polyarginine stretch expands the RNA binding specificity, and a minimal arginine cluster is required for optimal RRE RNA binding affinity, nuclear accumulation, and trans-activation.
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J Virol,
75,
2957-2971.
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E.Grahn,
N.J.Stonehouse,
C.J.Adams,
K.Fridborg,
L.Beigelman,
J.Matulic-Adamic,
S.L.Warriner,
P.G.Stockley,
and
L.Liljas
(2000).
Deletion of a single hydrogen bonding atom from the MS2 RNA operator leads to dramatic rearrangements at the RNA-coat protein interface.
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Nucleic Acids Res,
28,
4611-4616.
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PDB codes:
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K.Tars,
K.Fridborg,
M.Bundule,
and
L.Liljas
(2000).
Structure determination of bacteriophage PP7 from Pseudomonas aeruginosa: from poor data to a good map.
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Acta Crystallogr D Biol Crystallogr,
56,
398-405.
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PDB code:
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D.S.Peabody,
and
A.Chakerian
(1999).
Asymmetric contributions to RNA binding by the Thr(45) residues of the MS2 coat protein dimer.
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J Biol Chem,
274,
25403-25410.
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E.Grahn,
N.J.Stonehouse,
J.B.Murray,
S.van den Worm,
K.Valegård,
K.Fridborg,
P.G.Stockley,
and
L.Liljas
(1999).
Crystallographic studies of RNA hairpins in complexes with recombinant MS2 capsids: implications for binding requirements.
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RNA,
5,
131-138.
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PDB codes:
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H.Lago,
S.A.Fonseca,
J.B.Murray,
N.J.Stonehouse,
and
P.G.Stockley
(1998).
Dissecting the key recognition features of the MS2 bacteriophage translational repression complex.
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Nucleic Acids Res,
26,
1337-1344.
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M.A.Convery,
S.Rowsell,
N.J.Stonehouse,
A.D.Ellington,
I.Hirao,
J.B.Murray,
D.S.Peabody,
S.E.Phillips,
and
P.G.Stockley
(1998).
Crystal structure of an RNA aptamer-protein complex at 2.8 A resolution.
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Nat Struct Biol,
5,
133-139.
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PDB code:
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M.S.Chapman
(1998).
Watching one's P's and Q's: promiscuity, plasticity, and quasiequivalence in a T = 1 virus.
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Biophys J,
74,
639-644.
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R.N.De Guzman,
R.B.Turner,
and
M.F.Summers
(1998).
Protein-RNA recognition.
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Biopolymers,
48,
181-195.
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S.H.van den Worm,
N.J.Stonehouse,
K.Valegârd,
J.B.Murray,
C.Walton,
K.Fridborg,
P.G.Stockley,
and
L.Liljas
(1998).
Crystal structures of MS2 coat protein mutants in complex with wild-type RNA operator fragments.
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Nucleic Acids Res,
26,
1345-1351.
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PDB codes:
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S.Rowsell,
N.J.Stonehouse,
M.A.Convery,
C.J.Adams,
A.D.Ellington,
I.Hirao,
D.S.Peabody,
P.G.Stockley,
and
S.E.Phillips
(1998).
Crystal structures of a series of RNA aptamers complexed to the same protein target.
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Nat Struct Biol,
5,
970-975.
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PDB codes:
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M.Spingola,
and
D.S.Peabody
(1997).
MS2 coat protein mutants which bind Qbeta RNA.
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Nucleic Acids Res,
25,
2808-2815.
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S.Wang,
H.L.True,
E.M.Seitz,
K.A.Bennett,
D.E.Fouts,
J.F.Gardner,
and
D.W.Celander
(1997).
Direct genetic selection of two classes of R17/MS2 coat proteins with altered capsid assembly properties and expanded RNA-binding activities.
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Nucleic Acids Res,
25,
1649-1657.
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C.Z.Ni,
C.A.White,
R.S.Mitchell,
J.Wickersham,
R.Kodandapani,
D.S.Peabody,
and
K.R.Ely
(1996).
Crystal structure of the coat protein from the GA bacteriophage: model of the unassembled dimer.
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Protein Sci,
5,
2485-2493.
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PDB code:
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D.S.Peabody,
and
F.Lim
(1996).
Complementation of RNA binding site mutations in MS2 coat protein heterodimers.
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Nucleic Acids Res,
24,
2352-2359.
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K.A.LeCuyer,
L.S.Behlen,
and
O.C.Uhlenbeck
(1996).
Mutagenesis of a stacking contact in the MS2 coat protein-RNA complex.
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EMBO J,
15,
6847-6853.
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K.Nagai
(1996).
RNA-protein complexes.
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Curr Opin Struct Biol,
6,
53-61.
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R.Golmohammadi,
K.Fridborg,
M.Bundule,
K.Valegård,
and
L.Liljas
(1996).
The crystal structure of bacteriophage Q beta at 3.5 A resolution.
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Structure,
4,
543-554.
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PDB code:
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C.Z.Ni,
R.Syed,
R.Kodandapani,
J.Wickersham,
D.S.Peabody,
and
K.R.Ely
(1995).
Crystal structure of the MS2 coat protein dimer: implications for RNA binding and virus assembly.
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Structure,
3,
255-263.
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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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