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PDBsum entry 3a4c
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Cell cycle, replication
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PDB id
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3a4c
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Contents |
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* Residue conservation analysis
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Protein Sci
18:2252-2264
(2009)
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PubMed id:
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Structure of the Cdt1 C-terminal domain: conservation of the winged helix fold in replication licensing factors.
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B.I.Khayrutdinov,
W.J.Bae,
Y.M.Yun,
J.H.Lee,
T.Tsuyama,
J.J.Kim,
E.Hwang,
K.S.Ryu,
H.K.Cheong,
C.Cheong,
J.S.Ko,
T.Enomoto,
P.A.Karplus,
P.Güntert,
S.Tada,
Y.H.Jeon,
Y.Cho.
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ABSTRACT
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In eukaryotic replication licensing, Cdt1 plays a key role by recruiting the
MCM2-7 complex onto the origin of chromosome. The C-terminal domain of mouse
Cdt1 (mCdt1C), the most conserved region in Cdt1, is essential for licensing and
directly interacts with the MCM2-7 complex. We have determined the structures of
mCdt1CS (mCdt1C_small; residues 452 to 557) and mCdt1CL (mCdt1C_large; residues
420 to 557) using X-ray crystallography and solution NMR spectroscopy,
respectively. While the N-terminal 31 residues of mCdt1CL form a flexible loop
with a short helix near the middle, the rest of mCdt1C folds into a winged helix
structure. Together with the middle domain of mouse Cdt1 (mCdt1M, residues
172-368), this study reveals that Cdt1 is formed with a tandem repeat of the
winged helix domain. The winged helix fold is also conserved in other licensing
factors including archaeal ORC and Cdc6, which supports an idea that these
replication initiators may have evolved from a common ancestor. Based on the
structure of mCdt1C, in conjunction with the biochemical analysis, we propose a
binding site for the MCM complex within the mCdt1C.
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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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L.N.Truong,
and
X.Wu
(2011).
Prevention of DNA re-replication in eukaryotic cells.
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J Mol Cell Biol,
3,
13-22.
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J.Jee,
T.Mizuno,
K.Kamada,
H.Tochio,
Y.Chiba,
K.Yanagi,
G.Yasuda,
H.Hiroaki,
F.Hanaoka,
and
M.Shirakawa
(2010).
Structure and mutagenesis studies of the C-terminal region of licensing factor Cdt1 enable the identification of key residues for binding to replicative helicase Mcm proteins.
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J Biol Chem,
285,
15931-15940.
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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
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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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