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Gene regulation
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PDB id
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1d8l
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* Residue conservation analysis
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Enzyme class:
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E.C.3.6.4.12
- Dna helicase.
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Reaction:
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ATP + H2O = ADP + phosphate
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ATP
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+
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H(2)O
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=
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ADP
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+
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phosphate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Gene Ontology (GO) functional annotation
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Biological process
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DNA repair
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2 terms
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Biochemical function
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DNA binding
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4 terms
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DOI no:
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J Mol Biol
298:407-416
(2000)
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PubMed id:
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Modulation of RuvB function by the mobile domain III of the Holliday junction recognition protein RuvA.
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T.Nishino,
H.Iwasaki,
M.Kataoka,
M.Ariyoshi,
T.Fujita,
H.Shinagawa,
K.Morikawa.
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ABSTRACT
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In prokaryotes, RuvA-RuvB complexes play a crucial role in the migration of the
Holliday junction, which is a key intermediate of homologous recombination. RuvA
binds to the Holliday junction and enhances the ATPase activity of RuvB required
for branch migration. RuvA adopts a unique domain structure, which assembles
into a tetrameric molecule. The previous mutational and proteolytic analyses
suggested that mutations in a carboxyl-terminal domain (domain III) impair
binding of RuvA to RuvB. In order to clarify the functional role of each domain
in vitro, we established the recombinant expression systems, which allow us to
analyze structural and biochemical properties of each domain separately. A
small-angle X-ray scattering solution study, combined with X-ray
crystallographic analyses, was applied to the tetrameric full-length RuvA and
its tetrameric NH2 region (domains I and II) lacking the domain III. These
results demonstrated that domain III can be completely separate from the
tetrameric major core of the NH2 region and freely mobile in solution, through a
remarkably flexible loop. Biochemical analyses indicated that domain III not
only interacts with RuvB, but also modulates its ATPase activity. This
modulation may facilitate the dynamic coupling between RuvA and RuvB during
branch migration.
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Selected figure(s)
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Figure 3.
Figure 3. Superposition of the full-length RuvA (white) and
the NH2 region crystal structures (yellow). The worm models were
generated by GRASP [Nicholls 1993].
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Figure 8.
Figure 8. Functional model of RuvA, RuvB, and Holliday
junction complex. The NH2 region, which binds Holliday junction,
is represented by four ovals. Domain III, represented by a
circle, is tethered to the NH2 region through a flexible loop.
The RuvB ring, encircling DNA, interacts with domain III to
modulate ATPase activity during branch migration.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2000,
298,
407-416)
copyright 2000.
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Figures were
selected
by an automated process.
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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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F.Wang,
Y.Yang,
T.R.Singh,
V.Busygina,
R.Guo,
K.Wan,
W.Wang,
P.Sung,
A.R.Meetei,
and
M.Lei
(2010).
Crystal structures of RMI1 and RMI2, two OB-fold regulatory subunits of the BLM complex.
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Structure, 18,
1159-1170.
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PDB codes:
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T.Oyama,
H.Oka,
K.Mayanagi,
T.Shirai,
K.Matoba,
R.Fujikane,
Y.Ishino,
and
K.Morikawa
(2009).
Atomic structures and functional implications of the archaeal RecQ-like helicase Hjm.
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BMC Struct Biol, 9,
2.
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PDB codes:
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Z.Baharoglu,
A.S.Bradley,
M.Le Masson,
I.Tsaneva,
and
B.Michel
(2008).
ruvA Mutants that resolve Holliday junctions but do not reverse replication forks.
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PLoS Genet, 4,
e1000012.
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Y.W.Han,
T.Tani,
M.Hayashi,
T.Hishida,
H.Iwasaki,
H.Shinagawa,
and
Y.Harada
(2006).
Direct observation of DNA rotation during branch migration of Holliday junction DNA by Escherichia coli RuvA-RuvB protein complex.
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Proc Natl Acad Sci U S A, 103,
11544-11548.
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C.V.Privezentzev,
A.Keeley,
B.Sigala,
and
I.R.Tsaneva
(2005).
The role of RuvA octamerization for RuvAB function in vitro and in vivo.
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J Biol Chem, 280,
3365-3375.
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T.Ohnishi,
T.Hishida,
Y.Harada,
H.Iwasaki,
and
H.Shinagawa
(2005).
Structure-function analysis of the three domains of RuvB DNA motor protein.
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J Biol Chem, 280,
30504-30510.
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K.Yamada,
M.Ariyoshi,
and
K.Morikawa
(2004).
Three-dimensional structural views of branch migration and resolution in DNA homologous recombination.
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Curr Opin Struct Biol, 14,
130-137.
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R.Amit,
O.Gileadi,
and
J.Stavans
(2004).
Direct observation of RuvAB-catalyzed branch migration of single Holliday junctions.
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Proc Natl Acad Sci U S A, 101,
11605-11610.
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S.M.Ingleston,
M.J.Dickman,
J.A.Grasby,
D.P.Hornby,
G.J.Sharples,
and
R.G.Lloyd
(2002).
Holliday junction binding and processing by the RuvA protein of Mycoplasma pneumoniae.
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Eur J Biochem, 269,
1525-1533.
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K.Yamada,
N.Kunishima,
K.Mayanagi,
T.Ohnishi,
T.Nishino,
H.Iwasaki,
H.Shinagawa,
and
K.Morikawa
(2001).
Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8.
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Proc Natl Acad Sci U S A, 98,
1442-1447.
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PDB code:
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M.Ariyoshi,
T.Nishino,
H.Iwasaki,
H.Shinagawa,
and
K.Morikawa
(2000).
Crystal structure of the holliday junction DNA in complex with a single RuvA tetramer.
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| |
Proc Natl Acad Sci U S A, 97,
8257-8262.
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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
codes are
shown on the right.
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