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PDBsum entry 2vqc
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DNA binding protein
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PDB id
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2vqc
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References listed in PDB file
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Key reference
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Title
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Cysteine usage in sulfolobus spindle-Shaped virus 1 and extension to hyperthermophilic viruses in general.
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Authors
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S.K.Menon,
W.S.Maaty,
G.J.Corn,
S.C.Kwok,
B.J.Eilers,
P.Kraft,
E.Gillitzer,
M.J.Young,
B.Bothner,
C.M.Lawrence.
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Ref.
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Virology, 2008,
376,
270-278.
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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Fuselloviridae are ubiquitous crenarchaeal viruses found in high-temperature
acidic hot springs worldwide. The type virus, Sulfolobus spindle-shaped virus 1
(SSV1), has a double-stranded DNA genome that contains 34 open reading frames
(ORFs). Fuselloviral genomes show little similarity to other organisms,
generally precluding functional predictions. However, tertiary protein structure
can provide insight into protein function. We have thus undertaken a systematic
investigation of the SSV1 proteome and report here on the F112 gene product.
Biochemical, proteomic and structural studies reveal a monomeric intracellular
protein that adopts a winged helix DNA binding fold. Notably, the structure
contains an intrachain disulfide bond, prompting analysis of cysteine usage in
this and other hyperthermophilic viral genomes. The analysis supports a general
abundance of disulfide bonds in the intracellular proteins of hyperthermophilic
viruses, and reveals decreased cysteine content in the membrane proteins of
hyperthermophilic viruses infecting Sulfolobales. The evolutionary implications
of the SSV1 distribution are discussed.
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