Summary for 2ZXX
| Entry DOI | 10.2210/pdb2zxx/pdb |
| Descriptor | Geminin, DNA replication factor Cdt1 (3 entities in total) |
| Functional Keywords | coiled-coil, cell cycle, coiled coil, dna replication inhibitor, phosphoprotein, dna replication, dna-binding, nucleus, proto-oncogene, ubl conjugation, cell cycle-replication complex, cell cycle/replication |
| Biological source | Mus musculus (mouse) More |
| Cellular location | Nucleus: Q8R4E9 |
| Total number of polymer chains | 6 |
| Total formula weight | 84026.76 |
| Authors | Cho, Y.,Lee, C.,Hong, B.S.,Choi, J.M. (deposition date: 2009-01-08, release date: 2009-02-17, Last modification date: 2024-11-20) |
| Primary citation | Lee, C.,Hong, B.S.,Choi, J.M.,Kim, Y.,Watanabe, S.,Ishimi, Y.,Enomoto, T.,Tada, S.,Kim, Y.,Cho, Y. Structural basis for inhibition of the replication licensing factor Cdt1 by geminin Nature, 430:913-917, 2004 Cited by PubMed Abstract: To maintain chromosome stability in eukaryotic cells, replication origins must be licensed by loading mini-chromosome maintenance (MCM2-7) complexes once and only once per cell cycle. This licensing control is achieved through the activities of geminin and cyclin-dependent kinases. Geminin binds tightly to Cdt1, an essential component of the replication licensing system, and prevents the inappropriate reinitiation of replication on an already fired origin. The inhibitory effect of geminin is thought to prevent the interaction between Cdt1 and the MCM helicase. Here we describe the crystal structure of the mouse geminin-Cdt1 complex using tGeminin (residues 79-157, truncated geminin) and tCdt1 (residues 172-368, truncated Cdt1). The amino-terminal region of a coiled-coil dimer of tGeminin interacts with both N-terminal and carboxy-terminal parts of tCdt1. The primary interface relies on the steric complementarity between the tGeminin dimer and the hydrophobic face of the two short N-terminal helices of tCdt1 and, in particular, Pro 181, Ala 182, Tyr 183, Phe 186 and Leu 189. The crystal structure, in conjunction with our biochemical data, indicates that the N-terminal region of tGeminin might be required to anchor tCdt1, and the C-terminal region of tGeminin prevents access of the MCM complex to tCdt1 through steric hindrance. PubMed: 15286659DOI: 10.1038/nature02813 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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