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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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Crystal structure of the yeast mitochondrial holliday junction resolvase, ydc2
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Structure:
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Hypothetical 30.2 kd protein c25g10.02 in chromosome i. Chain: a, b. Engineered: yes
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Source:
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Schizosaccharomyces pombe. Fission yeast. Organism_taxid: 4896. Gene: spac25g10.02. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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Resolution:
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2.30Å
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R-factor:
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0.238
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R-free:
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0.270
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Authors:
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S.Ceschini,A.Keeley,M.S.B.Mcalister,M.Oram,J.Phelan,L.H.Pearl, I.R.Tsaneva,T.E.Barrett
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Key ref:
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S.Ceschini
et al.
(2001).
Crystal structure of the fission yeast mitochondrial Holliday junction resolvase Ydc2.
EMBO J,
20,
6601-6611.
PubMed id:
DOI:
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Date:
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08-Nov-01
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Release date:
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28-Nov-01
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, B:
E.C.3.1.21.10
- crossover junction endodeoxyribonuclease.
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DOI no:
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EMBO J
20:6601-6611
(2001)
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PubMed id:
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Crystal structure of the fission yeast mitochondrial Holliday junction resolvase Ydc2.
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S.Ceschini,
A.Keeley,
M.S.McAlister,
M.Oram,
J.Phelan,
L.H.Pearl,
I.R.Tsaneva,
T.E.Barrett.
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ABSTRACT
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Resolution of Holliday junctions into separate DNA duplexes requires enzymatic
cleavage of an equivalent strand from each contributing duplex at or close to
the point of strand exchange. Diverse Holliday junction-resolving enzymes have
been identified in bacteria, bacteriophages, archaea and pox viruses, but the
only eukaryotic examples identified so far are those from fungal mitochondria.
We have now determined the crystal structure of Ydc2 (also known as SpCce1), a
Holliday junction resolvase from the fission yeast Schizosaccharomyces pombe
that is involved in the maintenance of mitochondrial DNA. This first structure
of a eukaryotic Holliday junction resolvase confirms a distant evolutionary
relationship to the bacterial RuvC family, but reveals structural features which
are unique to the eukaryotic enzymes. Detailed analysis of the dimeric structure
suggests mechanisms for junction isomerization and communication between the two
active sites, and together with site-directed mutagenesis identifies residues
involved in catalysis.
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Selected figure(s)
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Figure 5.
Figure 5 Active site variability and communication. (A)
Superposition of the active sites from the metal-ion bound
monomer (yellow) and the metal-free monomer (green). Significant
changes in conformation of side chains and in the order of
adjacent segments of the polypeptide chain occur as a result of
metal ion binding. (B) A pathway for communication between the
two active sites is provided by the direct interaction of the
N-termini of helix 4 at the dimer interface. These are directly
linked to the flexible 'pin' segments, which in turn connect to
the active site metal ion ligand Glu117. Changes in the
conformation of one active site would be communicated to the
other site via this pathway, and could mediate the positive
cooperativity observed between the first and second strand
cleavage reactions.
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Figure 6.
Figure 6 Holliday junction complex. Model of a productive Ydc2
-Holliday junction complex. A model Holliday junction in an
open, approximately square-planar conformation (transparent CPK
model) can be docked onto the basic face of the Ydc2 dimer,
bringing the scissile phosphodiester bonds close to the acidic
cluster and the metal ion-binding site (red). The 'pin' and
N-terminus of helix 4 that protrude from this face are
accommodated by the centre of the open junction, but would
prevent binding of the junction in a stacked-X conformation.
Scissile phosphate groups are highlighted in yellow.
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2001,
20,
6601-6611)
copyright 2001.
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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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W.Yang
(2011).
Nucleases: diversity of structure, function and mechanism.
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Q Rev Biophys,
44,
1.
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C.D.Duncan,
and
K.M.Weeks
(2010).
The Mrs1 splicing factor binds the bI3 group I intron at each of two tetraloop-receptor motifs.
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PLoS One,
5,
e8983.
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E.M.Turk,
and
M.G.Caprara
(2010).
Splicing of yeast aI5beta group I intron requires SUV3 to recycle MRS1 via mitochondrial degradosome-promoted decay of excised intron ribonucleoprotein (RNP).
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J Biol Chem,
285,
8585-8594.
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J.M.Svendsen,
and
J.W.Harper
(2010).
GEN1/Yen1 and the SLX4 complex: Solutions to the problem of Holliday junction resolution.
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Genes Dev,
24,
521-536.
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B.Dalhus,
A.S.Arvai,
I.Rosnes,
..E.Olsen,
P.H.Backe,
I.Alseth,
H.Gao,
W.Cao,
J.A.Tainer,
and
M.Bjørås
(2009).
Structures of endonuclease V with DNA reveal initiation of deaminated adenine repair.
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Nat Struct Mol Biol,
16,
138-143.
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PDB codes:
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F.Osman,
L.Gaskell,
and
M.C.Whitby
(2009).
Efficient second strand cleavage during holliday junction resolution by RuvC requires both increased junction flexibility and an exposed 5' phosphate.
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PLoS ONE,
4,
e5347.
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M.Nowotny
(2009).
Retroviral integrase superfamily: the structural perspective.
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EMBO Rep,
10,
144-151.
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R.Suzuki,
H.Shindo,
A.Tase,
Y.Kikuchi,
M.Shimizu,
and
T.Yamazaki
(2009).
Solution structures and DNA binding properties of the N-terminal SAP domains of SUMO E3 ligases from Saccharomyces cerevisiae and Oryza sativa.
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Proteins,
75,
336-347.
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PDB codes:
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A.C.Déclais,
and
D.M.Lilley
(2008).
New insight into the recognition of branched DNA structure by junction-resolving enzymes.
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Curr Opin Struct Biol,
18,
86-95.
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C.Biertümpfel,
W.Yang,
and
D.Suck
(2007).
Crystal structure of T4 endonuclease VII resolving a Holliday junction.
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Nature,
449,
616-620.
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PDB codes:
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E.Karakas,
J.J.Truglio,
D.Croteau,
B.Rhau,
L.Wang,
B.Van Houten,
and
C.Kisker
(2007).
Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad.
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EMBO J,
26,
613-622.
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PDB codes:
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M.J.Culyba,
N.Minkah,
Y.Hwang,
O.M.Benhamou,
and
F.D.Bushman
(2007).
DNA branch nuclease activity of vaccinia A22 resolvase.
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J Biol Chem,
282,
34644-34652.
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J.Nosek,
L.Tomaska,
M.Bolotin-Fukuhara,
and
I.Miyakawa
(2006).
Mitochondrial chromosome structure: an insight from analysis of complete yeast genomes.
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FEMS Yeast Res,
6,
356-370.
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R.Macmaster,
S.Sedelnikova,
P.J.Baker,
E.L.Bolt,
R.G.Lloyd,
and
J.B.Rafferty
(2006).
RusA Holliday junction resolvase: DNA complex structure--insights into selectivity and specificity.
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Nucleic Acids Res,
34,
5577-5584.
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PDB codes:
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F.A.Curtis,
P.Reed,
and
G.J.Sharples
(2005).
Evolution of a phage RuvC endonuclease for resolution of both Holliday and branched DNA junctions.
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Mol Microbiol,
55,
1332-1345.
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M.Nowotny,
S.A.Gaidamakov,
R.J.Crouch,
and
W.Yang
(2005).
Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate specificity and metal-dependent catalysis.
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Cell,
121,
1005-1016.
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PDB codes:
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N.McGregor,
S.Ayora,
S.Sedelnikova,
B.Carrasco,
J.C.Alonso,
P.Thaw,
and
J.Rafferty
(2005).
The structure of Bacillus subtilis RecU Holliday junction resolvase and its role in substrate selection and sequence-specific cleavage.
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Structure,
13,
1341-1351.
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PDB code:
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..Knizewski,
and
K.Ginalski
(2005).
Bacillus subtilis YkuK protein is distantly related to RNase H.
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FEMS Microbiol Lett,
251,
341-346.
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C.L.Middleton,
J.L.Parker,
D.J.Richard,
M.F.White,
and
C.S.Bond
(2004).
Substrate recognition and catalysis by the Holliday junction resolving enzyme Hje.
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Nucleic Acids Res,
32,
5442-5451.
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PDB codes:
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S.Okubo,
F.Hara,
Y.Tsuchida,
S.Shimotakahara,
S.Suzuki,
H.Hatanaka,
S.Yokoyama,
H.Tanaka,
H.Yasuda,
and
H.Shindo
(2004).
NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers.
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J Biol Chem,
279,
31455-31461.
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PDB code:
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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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A.C.Déclais,
J.M.Fogg,
A.D.Freeman,
F.Coste,
J.M.Hadden,
S.E.Phillips,
and
D.M.Lilley
(2003).
The complex between a four-way DNA junction and T7 endonuclease I.
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EMBO J,
22,
1398-1409.
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B.Sigala,
and
I.R.Tsaneva
(2003).
Functional dissection of the Schizosaccharomyces pombe Holliday junction resolvase Ydc2: in vivo role in mitochondrial DNA maintenance.
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Eur J Biochem,
270,
2837-2847.
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J.S.Ahn,
and
M.C.Whitby
(2003).
The role of the SAP motif in promoting Holliday junction binding and resolution by SpCCE1.
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J Biol Chem,
278,
29121-29129.
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T.A.Muranova,
S.E.Sedelnikova,
P.M.Leonard,
A.Pasquo,
E.L.Bolt,
R.G.Lloyd,
and
J.B.Rafferty
(2003).
Crystallization of RusA Holliday junction resolvase from Escherichia coli.
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Acta Crystallogr D Biol Crystallogr,
59,
2262-2264.
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G.J.Sharples,
E.L.Bolt,
and
R.G.Lloyd
(2002).
RusA proteins from the extreme thermophile Aquifex aeolicus and lactococcal phage r1t resolve Holliday junctions.
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Mol Microbiol,
44,
549-559.
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J.H.Thorpe,
S.C.Teixeira,
B.C.Gale,
and
C.J.Cardin
(2002).
Structural characterization of a new crystal form of the four-way Holliday junction formed by the DNA sequence d(CCGGTACCGG)2: sequence versus lattice?
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Acta Crystallogr D Biol Crystallogr,
58,
567-569.
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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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}
}
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