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135 a.a.
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191 a.a.
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308 a.a.
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Ruva-ruvb complex
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Structure:
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Holliday junction DNA helicase ruva. Chain: a, b. Engineered: yes. Ruvb. Chain: c. Fragment: residues 1-312. Engineered: yes. Mutation: yes
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Source:
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Thermus thermophilus. Organism_taxid: 274. Gene: ruva. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Gene: ruvb.
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Biol. unit:
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Dodecamer (from PDB file)
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Resolution:
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3.30Å
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R-factor:
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0.268
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R-free:
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0.335
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Authors:
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K.Yamada,T.Miyata,D.Tsuchiya,T.Oyama,Y.Fujiwara,T.Ohnishi,H.Iwasaki, H.Shinagawa,M.Ariyoshi,K.Mayanagi,K.Morikawa
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Key ref:
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K.Yamada
et al.
(2002).
Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery.
Mol Cell,
10,
671-681.
PubMed id:
DOI:
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Date:
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04-Jul-02
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Release date:
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06-Nov-02
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PROCHECK
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Headers
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References
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Q9F1Q3
(RUVA_THET8) -
Holliday junction branch migration complex subunit RuvA from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
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Seq: Struc:
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191 a.a.
135 a.a.
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DOI no:
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Mol Cell
10:671-681
(2002)
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PubMed id:
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Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery.
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K.Yamada,
T.Miyata,
D.Tsuchiya,
T.Oyama,
Y.Fujiwara,
T.Ohnishi,
H.Iwasaki,
H.Shinagawa,
M.Ariyoshi,
K.Mayanagi,
K.Morikawa.
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ABSTRACT
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We present the X-ray structure of the RuvA-RuvB complex, which plays a crucial
role in ATP-dependent branch migration. Two RuvA tetramers form the symmetric
and closed octameric shell, where four RuvA domain IIIs spring out in the two
opposite directions to be individually caught by a single RuvB. The binding of
domain III deforms the protruding beta hairpin in the N-terminal domain of RuvB
and thereby appears to induce a functional and less symmetric RuvB hexameric
ring. The model of the RuvA-RuvB junction DNA ternary complex, constructed by
fitting the X-ray structure into the averaged electron microscopic images of the
RuvA-RuvB junction, appears to be more compatible with the branch migration mode
of a fixed RuvA-RuvB interaction than with a rotational interaction mode.
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Selected figure(s)
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Figure 4.
Figure 4. Averaged Electron Microscopic Image of the
RuvA-RuvB-Holliday Junction Ternary Complex and the
Corresponding Functional Atomic ModelThe IMAGIC program package
(van Heel et al., 1996) was used to cluster particle images and
to obtain class averages. The hypothetical model was constructed
by fitting the RuvA octameric core structure (yellow) and the
RuvB hexamer models (blue) into the averaged images, referring
to the hexameric oligomerization of the HslU protein similar to
RuvB (Sousa et al., 2000). One pair of subunits related in
each hexameric ring by the central 2-fold axis was replaced by
the two domain III (orange)-RuvB (magenta) complexes (see text).
Averaged electron microscopic images correspond to two
orthogonal views of the ternary complex. The 858 original
images were grouped into three major classes of averaged images,
and only two of them, (A) and (B), averaged from 171 and 370
electron microscopic images, are shown here. Note the good
coincidence of the images with the side (A) and end views (B) of
the RuvA octameric core structure. The resolutions of the
averaged images of (A) and (B) were estimated at 34 and 31
Å, respectively, from differential phase residuals. The
scale bar represents 100 Å.
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Figure 5.
Figure 5. Model of the Loading Process of the RuvA-RuvB
Complex on a Holliday JunctionEach of the three components in
this process was determined by X-ray analyses (forms I, II, and
III) or by an electron microscopic study (form IV). The RuvA
core region and domain III are colored by yellow and orange,
respectively. The RuvB subunit is depicted by a blue oval.
Red-trimmed ovals represent domain III bound to the RuvB
subunit. The RuvA-RuvB complex (form III) is regarded as the
preloading complex before forming the functional complex on a
Holliday junction (form IV). During the conversion from form III
to IV, the RuvB subunit that was previously connected with the
RuvA octameric core is no longer replaced by other partners.
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2002,
10,
671-681)
copyright 2002.
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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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A.P.Carter,
C.Cho,
L.Jin,
and
R.D.Vale
(2011).
Crystal structure of the dynein motor domain.
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Science,
331,
1159-1165.
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PDB code:
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R.Morita,
S.Nakane,
A.Shimada,
M.Inoue,
H.Iino,
T.Wakamatsu,
K.Fukui,
N.Nakagawa,
R.Masui,
and
S.Kuramitsu
(2010).
Molecular mechanisms of the whole DNA repair system: a comparison of bacterial and eukaryotic systems.
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J Nucleic Acids,
2010,
179594.
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J.Atkinson,
and
P.McGlynn
(2009).
Replication fork reversal and the maintenance of genome stability.
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Nucleic Acids Res,
37,
3475-3492.
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P.C.Burrows,
J.Schumacher,
S.Amartey,
T.Ghosh,
T.A.Burgis,
X.Zhang,
B.T.Nixon,
and
M.Buck
(2009).
Functional roles of the pre-sensor I insertion sequence in an AAA+ bacterial enhancer binding protein.
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Mol Microbiol,
73,
519-533.
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Q.Xu,
C.L.Rife,
D.Carlton,
M.D.Miller,
S.S.Krishna,
M.A.Elsliger,
P.Abdubek,
T.Astakhova,
H.J.Chiu,
T.Clayton,
L.Duan,
J.Feuerhelm,
S.K.Grzechnik,
J.Hale,
G.W.Han,
L.Jaroszewski,
K.K.Jin,
H.E.Klock,
M.W.Knuth,
A.Kumar,
D.McMullan,
A.T.Morse,
E.Nigoghossian,
L.Okach,
S.Oommachen,
J.Paulsen,
R.Reyes,
H.van den Bedem,
K.O.Hodgson,
J.Wooley,
A.M.Deacon,
A.Godzik,
S.A.Lesley,
and
I.A.Wilson
(2009).
Crystal structure of a novel archaeal AAA+ ATPase SSO1545 from Sulfolobus solfataricus.
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Proteins,
74,
1041-1049.
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PDB code:
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A.Kumar,
W.S.Joo,
G.Meinke,
S.Moine,
E.N.Naumova,
and
P.A.Bullock
(2008).
Evidence for a structural relationship between BRCT domains and the helicase domains of the replication initiators encoded by the Polyomaviridae and Papillomaviridae families of DNA tumor viruses.
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J Virol,
82,
8849-8862.
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A.S.Brewster,
G.Wang,
X.Yu,
W.B.Greenleaf,
J.M.Carazo,
M.Tjajadia,
M.G.Klein,
and
X.S.Chen
(2008).
Crystal structure of a near-full-length archaeal MCM: functional insights for an AAA+ hexameric helicase.
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Proc Natl Acad Sci U S A,
105,
20191-20196.
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PDB code:
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E.Torreira,
S.Jha,
J.R.López-Blanco,
E.Arias-Palomo,
P.Chacón,
C.Cañas,
S.Ayora,
A.Dutta,
and
O.Llorca
(2008).
Architecture of the pontin/reptin complex, essential in the assembly of several macromolecular complexes.
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Structure,
16,
1511-1520.
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I.J.Finkelstein,
and
E.C.Greene
(2008).
Single molecule studies of homologous recombination.
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Mol Biosyst,
4,
1094-1104.
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J.Snider,
G.Thibault,
and
W.A.Houry
(2008).
The AAA+ superfamily of functionally diverse proteins.
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Genome Biol,
9,
216.
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M.Le Masson,
Z.Baharoglu,
and
B.Michel
(2008).
ruvA and ruvB mutants specifically impaired for replication fork reversal.
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Mol Microbiol,
70,
537-548.
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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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I.Tato,
I.Matilla,
I.Arechaga,
S.Zunzunegui,
F.de la Cruz,
and
E.Cabezon
(2007).
The ATPase activity of the DNA transporter TrwB is modulated by protein TrwA: implications for a common assembly mechanism of DNA translocating motors.
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J Biol Chem,
282,
25569-25576.
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K.P.Hopfner,
and
J.Michaelis
(2007).
Mechanisms of nucleic acid translocases: lessons from structural biology and single-molecule biophysics.
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Curr Opin Struct Biol,
17,
87-95.
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A.Costa,
T.Pape,
M.van Heel,
P.Brick,
A.Patwardhan,
and
S.Onesti
(2006).
Structural basis of the Methanothermobacter thermautotrophicus MCM helicase activity.
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Nucleic Acids Res,
34,
5829-5838.
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J.P.Erzberger,
and
J.M.Berger
(2006).
Evolutionary relationships and structural mechanisms of AAA+ proteins.
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Annu Rev Biophys Biomol Struct,
35,
93.
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J.R.Prabu,
S.Thamotharan,
J.S.Khanduja,
E.Z.Alipio,
C.Y.Kim,
G.S.Waldo,
T.C.Terwilliger,
B.Segelke,
T.Lekin,
D.Toppani,
L.W.Hung,
M.Yu,
E.Bursey,
K.Muniyappa,
N.R.Chandra,
and
M.Vijayan
(2006).
Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
62,
731-734.
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PDB code:
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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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K.V.Kepple,
J.L.Boldt,
and
A.M.Segall
(2005).
Holliday junction-binding peptides inhibit distinct junction-processing enzymes.
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Proc Natl Acad Sci U S A,
102,
6867-6872.
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L.Aravind,
V.Anantharaman,
S.Balaji,
M.M.Babu,
and
L.M.Iyer
(2005).
The many faces of the helix-turn-helix domain: transcription regulation and beyond.
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FEMS Microbiol Rev,
29,
231-262.
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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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T.Tsurimoto,
A.Shinozaki,
M.Yano,
M.Seki,
and
T.Enomoto
(2005).
Human Werner helicase interacting protein 1 (WRNIP1) functions as a novel modulator for DNA polymerase delta.
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Genes Cells,
10,
13-22.
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C.Dennis,
A.Fedorov,
E.Käs,
L.Salomé,
and
M.Grigoriev
(2004).
RuvAB-directed branch migration of individual Holliday junctions is impeded by sequence heterology.
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EMBO J,
23,
2413-2422.
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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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T.Hishida,
Y.W.Han,
S.Fujimoto,
H.Iwasaki,
and
H.Shinagawa
(2004).
Direct evidence that a conserved arginine in RuvB AAA+ ATPase acts as an allosteric effector for the ATPase activity of the adjacent subunit in a hexamer.
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Proc Natl Acad Sci U S A,
101,
9573-9577.
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Y.Liu,
and
S.C.West
(2004).
Happy Hollidays: 40th anniversary of the Holliday junction.
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Nat Rev Mol Cell Biol,
5,
937-944.
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H.Yokoyama,
H.Kurumizaka,
S.Ikawa,
S.Yokoyama,
and
T.Shibata
(2003).
Holliday junction binding activity of the human Rad51B protein.
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J Biol Chem,
278,
2767-2772.
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J.A.James,
C.R.Escalante,
M.Yoon-Robarts,
T.A.Edwards,
R.M.Linden,
and
A.K.Aggarwal
(2003).
Crystal structure of the SF3 helicase from adeno-associated virus type 2.
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Structure,
11,
1025-1035.
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PDB code:
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S.C.West
(2003).
Molecular views of recombination proteins and their control.
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Nat Rev Mol Cell Biol,
4,
435-445.
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T.Hishida,
H.Iwasaki,
Y.W.Han,
T.Ohnishi,
and
H.Shinagawa
(2003).
Uncoupling of the ATPase activity from the branch migration activity of RuvAB protein complexes containing both wild-type and ATPase-defective RuvB proteins.
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Genes Cells,
8,
721-730.
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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
code is
shown on the right.
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}
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