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208 a.a.
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121 a.a.
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193 a.a.
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* Residue conservation analysis
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PDB id:
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Structural protein
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Title:
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Crystal structure of c. Tropicalis stn1-ten1 complex
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Structure:
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Protein stn1. Chain: a, c. Fragment: n-terminal fragment: unp residues 2-217. Engineered: yes. Protein ten1. Chain: b, d. Fragment: unp residues 2-123. Engineered: yes
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Source:
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Candida tropicalis mya-3404. Yeast. Organism_taxid: 294747. Strain: atcc mya-3404 / t1. Gene: ctrg_01841. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: ctrg_00988.
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Resolution:
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2.40Å
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R-factor:
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0.228
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R-free:
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0.265
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Authors:
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J.Sun,E.Y.Yu,Y.T.Yang,L.A.Confer,S.H.Sun,K.Wan,N.F.Lue,M.Lei
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Key ref:
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J.Sun
et al.
(2009).
Stn1-Ten1 is an Rpa2-Rpa3-like complex at telomeres.
Genes Dev,
23,
2900-2914.
PubMed id:
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Date:
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27-Oct-09
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Release date:
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22-Dec-09
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PROCHECK
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Headers
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References
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C5M7K9
(C5M7K9_CANTT) -
CST complex subunit Stn1 N-terminal domain-containing protein from Candida tropicalis (strain ATCC MYA-3404 / T1)
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Seq:
Struc:
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484 a.a.
208 a.a.
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Enzyme class:
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Chains A, B, C, D:
E.C.?
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Genes Dev
23:2900-2914
(2009)
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PubMed id:
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Stn1-Ten1 is an Rpa2-Rpa3-like complex at telomeres.
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J.Sun,
E.Y.Yu,
Y.Yang,
L.A.Confer,
S.H.Sun,
K.Wan,
N.F.Lue,
M.Lei.
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ABSTRACT
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In budding yeast, Cdc13, Stn1, and Ten1 form a heterotrimeric complex (CST) that
is essential for telomere protection and maintenance. Previous bioinformatics
analysis revealed a putative oligonucleotide/oligosaccharide-binding (OB) fold
at the N terminus of Stn1 (Stn1N) that shows limited sequence similarity to the
OB fold of Rpa2, a subunit of the eukaryotic ssDNA-binding protein complex
replication protein A (RPA). Here we present functional and structural analyses
of Stn1 and Ten1 from multiple budding and fission yeast. The crystal structure
of the Candida tropicalis Stn1N complexed with Ten1 demonstrates an
Rpa2N-Rpa3-like complex. In both structures, the OB folds of the two components
pack against each other through interactions between two C-terminal helices. The
structure of the C-terminal domain of Saccharomyces cerevisiae Stn1 (Stn1C) was
found to comprise two related winged helix-turn-helix (WH) motifs, one of which
is most similar to the WH motif at the C terminus of Rpa2, again supporting the
notion that Stn1 resembles Rpa2. The crystal structure of the fission yeast
Schizosaccharomyces pombe Stn1N-Ten1 complex exhibits a virtually identical
architecture as the C. tropicalis Stn1N-Ten1. Functional analyses of the Candida
albicans Stn1 and Ten1 proteins revealed critical roles for these proteins in
suppressing aberrant telomerase and recombination activities at telomeres.
Mutations that disrupt the Stn1-Ten1 interaction induce telomere uncapping and
abolish the telomere localization of Ten1. Collectively, our structural and
functional studies illustrate that, instead of being confined to budding yeast
telomeres, the CST complex may represent an evolutionarily conserved RPA-like
telomeric complex at the 3' overhangs that works in parallel with or instead of
the well-characterized POT1-TPP1/TEBPalpha-beta complex.
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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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J.Sun,
Y.Yang,
K.Wan,
N.Mao,
T.Y.Yu,
Y.C.Lin,
D.C.DeZwaan,
B.C.Freeman,
J.J.Lin,
N.F.Lue,
and
M.Lei
(2011).
Structural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase α.
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Cell Res,
21,
258-274.
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PDB codes:
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S.Li
(2011).
Cell-cycle-dependent telomere elongation by telomerase in budding yeast.
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Biosci Rep,
31,
169-177.
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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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G.D.Raffa,
D.Raimondo,
C.Sorino,
S.Cugusi,
G.Cenci,
S.Cacchione,
M.Gatti,
and
L.Ciapponi
(2010).
Verrocchio, a Drosophila OB fold-containing protein, is a component of the terminin telomere-capping complex.
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Genes Dev,
24,
1596-1601.
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K.A.Hoadley,
D.Xu,
Y.Xue,
K.A.Satyshur,
W.Wang,
and
J.L.Keck
(2010).
Structure and cellular roles of the RMI core complex from the bloom syndrome dissolvasome.
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Structure,
18,
1149-1158.
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PDB code:
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L.Subramanian,
and
T.M.Nakamura
(2010).
To fuse or not to fuse: how do checkpoint and DNA repair proteins maintain telomeres?
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Front Biosci,
15,
1105-1118.
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M.J.Giraud-Panis,
M.T.Teixeira,
V.Géli,
and
E.Gilson
(2010).
CST meets shelterin to keep telomeres in check.
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Mol Cell,
39,
665-676.
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M.Paschini,
E.K.Mandell,
and
V.Lundblad
(2010).
Structure prediction-driven genetics in Saccharomyces cerevisiae identifies an interface between the t-RPA proteins Stn1 and Ten1.
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Genetics,
185,
11-21.
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R.L.Flynn,
and
L.Zou
(2010).
Oligonucleotide/oligosaccharide-binding fold proteins: a growing family of genome guardians.
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Crit Rev Biochem Mol Biol,
45,
266-275.
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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
