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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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References listed in PDB file
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Key reference
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Title
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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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Authors
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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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Ref.
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Protein Sci, 2009,
18,
2252-2264.
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PubMed id
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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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