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PDBsum entry 3fbz
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Structural protein
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PDB id
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3fbz
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References listed in PDB file
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Key reference
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Title
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Acidianus filamentous virus 1 coat proteins display a helical fold spanning the filamentous archaeal viruses lineage.
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Authors
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A.Goulet,
S.Blangy,
P.Redder,
D.Prangishvili,
C.Felisberto-Rodrigues,
P.Forterre,
V.Campanacci,
C.Cambillau.
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Ref.
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Proc Natl Acad Sci U S A, 2009,
106,
21155-21160.
[DOI no: ]
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PubMed id
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Abstract
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Acidianus filamentous virus 1 (AFV1), a member of the Lipothrixviridae family,
infects the hyperthermophilic, acidophilic crenarchaeaon Acidianus hospitalis.
The virion, covered with a lipidic outer shell, is 9,100-A long and contains a
20.8-kb linear dsDNA genome. We have identified the two major coat proteins of
the virion (MCPs; 132 and 140 amino acids). They bind DNA and form filaments
when incubated with linear dsDNA. A C-terminal domain is identified in their
crystal structure with a four-helix-bundle fold. In the topological model of the
virion filament core, the genomic dsDNA superhelix wraps around the AFV1-132
basic protein, and the AFV1-140 basic N terminus binds genomic DNA, while its
lipophilic C-terminal domain is imbedded in the lipidic outer shell. The
four-helix bundle fold of the MCPs from AFV1 is identical to that of the coat
protein (CP) of Sulfolobus islandicus rod-shaped virus (SIRV), a member of the
Rudiviridae family. Despite low sequence identity between these proteins, their
high degree of structural similarity suggests that they could have derived from
a common ancestor and could thus define an yet undescribed viral lineage.
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Figure 2.
Crystal structure of ΔN_AFV1–132. (A) Ribbon
representation of ΔN_AFV1–132 crystal structure with a
rainbow color gradient from the N terminus (blue) to the C
terminus (red). Helices are sequentially labeled α1 to α4.
Tyr-51 is the first residue seen in the electron density map.
(B) ΔN_AFV1–132 crystal structure (cyan) superimposed onto
ΔN_SIRV-134 (residues 52–134) crystal structure (light green)
with a r.m.s deviation of 1.4 Å on the Cα backbone. (C
and D) Electrostatic surfaces of ΔN_AFV1–132 and
ΔN_SIRV-134, respectively, in the same orientation. Figs. were
created with Pymol, http://pymol.sourceforge.net/.
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Figure 3.
Crystal structure of AFV1–140. (A) AFV1–140 crystal
structure (gray) superimposed onto ΔN_AFV1–132 (cyan) with a
r.m.s deviation of 1.54 Å on the Cα backbone. Helices are
sequentially labeled α'1 to α'5. (B) Electrostatic surface in
the same orientation. (C) Head-to-tail dimer in which one chain
is shown as a gray ribbon and the other is represented as light
green surface. (D) Tetramer of the asymmetric unit is composed
of a dimer of dimers. Detergent molecules (β-OG) are
represented with orange surfaces. Figs. were created with Pymol.
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