3A4C

Crystal structure of cdt1 C terminal domain

Summary for 3A4C

• Entry DOI: 10.2210/pdb3a4c/pdb
• Related: 2KLO
• Descriptor: DNA replication factor Cdt1 (2 entities in total)
• Functional Keywords: alpha-beta structure, cell cycle, dna replication, dna-binding, nucleus, phosphoprotein, proto-oncogene, ubl conjugation, replication
• Biological source: Mus musculus (mouse)
• Cellular location: Nucleus : Q8R4E9
• Total number of polymer chains: 1
• Total formula weight: 12108.20

Authors

Cho, Y.,Lee, J.H. (deposition date: 2009-07-06, release date: 2009-10-13, Last modification date: 2025-04-30)

Primary citation

Khayrutdinov, B.I.,Bae, W.J.,Yun, Y.M.,Lee, J.H.,Tsuyama, T.,Kim, J.J.,Hwang, E.,Ryu, K.-S.,Cheong, H.-K.,Cheong, C.,Ko, J.-S.,Enomoto, T.,Karplus, P.A.,Guntert, P.,Tada, S.,Jeon, Y.H.,Cho, Y.
Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors
Protein Sci., 18:2252-2264, 2009

PubMed 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.

PubMed: 19722278
DOI: 10.1002/pro.236

Experimental method

X-RAY DIFFRACTION (1.889 Å)