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PDBsum entry 2vvf
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Viral protein
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PDB id
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2vvf
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References listed in PDB file
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Key reference
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Title
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Insights into virus evolution and membrane biogenesis from the structure of the marine lipid-Containing bacteriophage pm2.
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Authors
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N.G.Abrescia,
J.M.Grimes,
H.M.Kivelä,
R.Assenberg,
G.C.Sutton,
S.J.Butcher,
J.K.Bamford,
D.H.Bamford,
D.I.Stuart.
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Ref.
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Mol Cell, 2008,
31,
749-761.
[DOI no: ]
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PubMed id
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Abstract
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Recent, primarily structural observations indicate that related viruses,
harboring no sequence similarity, infect hosts of different domains of life. One
such clade of viruses, defined by common capsid architecture and coat protein
fold, is the so-called PRD1-adenovirus lineage. Here we report the structure of
the marine lipid-containing bacteriophage PM2 determined by crystallographic
analyses of the entire approximately 45 MDa virion and of the outer coat
proteins P1 and P2, revealing PM2 to be a primeval member of the PRD1-adenovirus
lineage with an icosahedral shell and canonical double beta barrel major coat
protein. The view of the lipid bilayer, richly decorated with membrane proteins,
constitutes a rare visualization of an in vivo membrane. The viral membrane
proteins P3 and P6 are organized into a lattice, suggesting a possible assembly
pathway to produce the mature virus.
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Figure 5.
Figure 5. Proteins P3 and P6
(A and B) Stereo pictures
of contiguous views of a portion of Cα traces of a P3 dimer
(magenta) and P6 (gold) fitted in the virus map (0.7σ, blue),
with SeMet difference Fourier (3.2σ, red) viewed orthogonally
to the virus surface.
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Figure 6.
Figure 6. Membrane and Genome Architecture
(A) (Left)
Slice through the PM2 electron density. The capsid is blue
(0.8σ), lipid headgroups cyan (0.25σ), acyl-chain region light
red (−1.3σ), and supercoiled DNA green (0.25σ). (Right)
Icosahedral electron density profile. Distances measured from
the particle center along the icosahedral 3-fold axis. IL and OL
mark the inner and outer membrane leaflets, respectively.
(B) Cartoon of PM2 membrane vesicle assembly. (1) Dimers of
protein P3 (magenta) and a monomer of protein P6 (gold) anchored
via transmembrane helices (data not shown) on a patch of
bacterial membrane. (2) Independent P3 dimers interact with
monomeric P6 forming the scaffold building block. (3) Three
building blocks come together by interaction of the P3 α1
helices to form a subassembly corresponding to an icosahedral
facet. (4) P6 molecules of two independent subassemblies
interact, facilitated by interaction with the supercoiled DNA
genome via P6 transmembrane helices (and possibly further
components such as P4). (5) This interaction generates a torque
across the membrane via the P6 helices (depicted as small
gold-colored rectangles), driving the curvature of the membrane.
(6) Recruitment of further P6-P3 subassemblies to the condensed
DNA genome leads to a correctly sized lipid vesicle coated with
P3 and P6, on which the outer protein capsid assembles.
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2008,
31,
749-761)
copyright 2008.
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