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Structure of the Cdt1 C-terminal domain: conservation of the winged helix fold in replication licensing factors.


ABSTRACT: 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.

SUBMITTER: Khayrutdinov BI 

PROVIDER: S-EPMC2788280 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature

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Structure of the Cdt1 C-terminal domain: conservation of the winged helix fold in replication licensing factors.

Khayrutdinov Bulat I BI   Bae Won Jin WJ   Yun Young Mi YM   Lee Jie Hye JH   Tsuyama Takashi T   Kim Jung Joo JJ   Hwang Eunha E   Ryu Kyoung-Seok KS   Cheong Hae-Kap HK   Cheong Chaejoon C   Ko Jung-Soon JS   Enomoto Takemi T   Karplus P Andrew PA   Güntert Peter P   Tada Shusuke S   Jeon Young Ho YH   Cho Yunje Y  

Protein science : a publication of the Protein Society 20091101 11


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-termina  ...[more]

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