ArticleProtein science : a publication of the Protein Society2009
Structure of the Cdt1 C-terminal domain: conservation of the winged helix fold in replication licensing factors.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 41 citations in OpenAlex.
- Overexpression of CDT1 inhibits cell cycle progression at S phase by interacting with the mini-chromosome maintenance complex and causes DNA damage.FEBS open bio · 2026Article
- SEC-SAXS/MC Ensemble Structural Studies of the Microtubule Binding Protein Cdt1 Show Monomeric, Folded-Over Conformations.Cytoskeleton (Hoboken, N.J.) · 2025Article
- SAXS/MC studies of the mixed-folded protein Cdt1 reveal monomeric, folded over conformations.bioRxiv : the preprint server for biology · 2024Article
- The Caenorhabditis elegans TDRD5/7-like protein, LOTR-1, interacts with the helicase ZNFX-1 to balance epigenetic signals in the germline.PLoS genetics · 2022Article
- Distinct and sequential re-replication barriers ensure precise genome duplication.PLoS genetics · 2020Article
- Moonlighting Proteins in the Fuzzy Logic of Cellular Metabolism.Molecules (Basel, Switzerland) · 2020Review
- Cryptic protein interactions regulate DNA replication initiation.Molecular microbiology · 2019Article
- Cdt1 variants reveal unanticipated aspects of interactions with cyclin/CDK and MCM important for normal genome replication.Molecular biology of the cell · 2018Article
- Cdt1 stabilizes kinetochore-microtubule attachments via an Aurora B kinase-dependent mechanism.The Journal of cell biology · 2018Article
- Review
- Rv0004 is a new essential member of the mycobacterial DNA replication machinery.PLoS genetics · 2017Article
- Cdt1 stabilizes an open MCM ring for helicase loading.Nature communications · 2017Article
- Mechanisms and regulation of DNA replication initiation in eukaryotes.Critical reviews in biochemistry and molecular biology · 2017Review
- The Temporal Regulation of S Phase Proteins During GAdvances in experimental medicine and biology · 2017Review
- Regulation and Function of Cdt1; A Key Factor in Cell Proliferation and Genome Stability.Genes · 2016Review
- Chromosome Duplication in Saccharomyces cerevisiae.Genetics · 2016Review
- Antimicrobial peptide protegrin-3 adopt an antiparallel dimer in the presence of DPC micelles: a high-resolution NMR study.Journal of biomolecular NMR · 2015Article
- Cryo-EM structure of a helicase loading intermediate containing ORC-Cdc6-Cdt1-MCM2-7 bound to DNA.Nature structural & molecular biology · 2013Article
- Helicase loading at chromosomal origins of replication.Cold Spring Harbor perspectives in biology · 2013Review
- Dynamic association of ORCA with prereplicative complex components regulates DNA replication initiation.Molecular and cellular biology · 2012Article
Corrections and comments
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Authors and funding
17 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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