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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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PDB id:
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| Name: |
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DNA binding protein
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Title:
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Structure of a DNA binding winged-helix protein, f-112, from sulfolobus spindle-shaped virus 1.
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Structure:
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Hypothetical 13.2 kda protein. Chain: a. Fragment: residues 2-112. Synonym: orf f-112, f-112. Engineered: yes
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Source:
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Sulfolobus virus-like particle ssv1. Organism_taxid: 244589. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.30Å
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R-factor:
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0.175
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R-free:
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0.199
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Authors:
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S.K.Menon,P.Kraft,G.J.Corn,B.Wiedenheft,M.J.Young,C.M.Lawrence
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Key ref:
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S.K.Menon
et al.
(2008).
Cysteine usage in Sulfolobus spindle-shaped virus 1 and extension to hyperthermophilic viruses in general.
Virology,
376,
270-278.
PubMed id:
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Date:
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12-Mar-08
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Release date:
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06-May-08
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Supersedes:
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PROCHECK
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Headers
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References
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P20220
(F112_SSV1) -
Protein F-112 from Sulfolobus spindle-shape virus 1
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Seq:
Struc:
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112 a.a.
70 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Virology
376:270-278
(2008)
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PubMed id:
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Cysteine usage in Sulfolobus spindle-shaped virus 1 and extension to hyperthermophilic viruses in general.
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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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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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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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A.Goulet,
M.Pina,
P.Redder,
D.Prangishvili,
L.Vera,
J.Lichière,
N.Leulliot,
H.van Tilbeurgh,
M.Ortiz-Lombardia,
V.Campanacci,
and
C.Cambillau
(2010).
ORF157 from the archaeal virus Acidianus filamentous virus 1 defines a new class of nuclease.
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J Virol,
84,
5025-5031.
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PDB codes:
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S.K.Menon,
B.J.Eilers,
M.J.Young,
and
C.M.Lawrence
(2010).
The crystal structure of D212 from sulfolobus spindle-shaped virus ragged hills reveals a new member of the PD-(D/E)XK nuclease superfamily.
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J Virol,
84,
5890-5897.
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PDB code:
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A.Goulet,
S.Spinelli,
S.Blangy,
H.van Tilbeurgh,
N.Leulliot,
T.Basta,
D.Prangishvili,
C.Cambillau,
and
V.Campanacci
(2009).
The thermo- and acido-stable ORF-99 from the archaeal virus AFV1.
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Protein Sci,
18,
1316-1320.
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PDB codes:
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C.M.Lawrence,
S.Menon,
B.J.Eilers,
B.Bothner,
R.Khayat,
T.Douglas,
and
M.J.Young
(2009).
Structural and functional studies of archaeal viruses.
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J Biol Chem,
284,
12599-12603.
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P.Redder,
X.Peng,
K.Brügger,
S.A.Shah,
F.Roesch,
B.Greve,
Q.She,
C.Schleper,
P.Forterre,
R.A.Garrett,
and
D.Prangishvili
(2009).
Four newly isolated fuselloviruses from extreme geothermal environments reveal unusual morphologies and a possible interviral recombination mechanism.
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Environ Microbiol,
11,
2849-2862.
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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
codes are
shown on the right.
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Links
