2KLQ
The solution structure of CBD of human MCM6
Summary for 2KLQ
Entry DOI | 10.2210/pdb2klq/pdb |
NMR Information | BMRB: 16396 |
Descriptor | DNA replication licensing factor MCM6 (1 entity in total) |
Functional Keywords | dna replication, pre-rc, mcm6, cdt1, cbd structure, atp-binding, cell cycle, dna-binding, nucleotide-binding, nucleus, phosphoprotein, polymorphism, transcription, transcription regulation, replication |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus: Q14566 |
Total number of polymer chains | 1 |
Total formula weight | 13303.88 |
Authors | |
Primary citation | Wei, Z.,Liu, C.,Wu, X.,Xu, N.,Zhou, B.,Liang, C.,Zhu, G. Characterization and structure determination of the Cdt1 binding domain of human minichromosome maintenance (Mcm) 6 J.Biol.Chem., 285:12469-12473, 2010 Cited by PubMed Abstract: The minichromosome maintenance (Mcm) 2-7 complex is the replicative helicase in eukaryotic species, and it plays essential roles in the initiation and elongation phases of DNA replication. During late M and early G(1), the Mcm2-7 complex is loaded onto chromatin to form prereplicative complex in a Cdt1-dependent manner. However, the detailed molecular mechanism of this loading process is still elusive. In this study, we demonstrate that the previously uncharacterized C-terminal domain of human Mcm6 is the Cdt1 binding domain (CBD) and present its high resolution NMR structure. The structure of CBD exhibits a typical "winged helix" fold that is generally involved in protein-nucleic acid interaction. Nevertheless, the CBD failed to interact with DNA in our studies, indicating that it is specific for protein-protein interaction. The CBD-Cdt1 interaction involves the helix-turn-helix motif of CBD. The results reported here provide insight into the molecular mechanism of Mcm2-7 chromatin loading and prereplicative complex assembly. PubMed: 20202939DOI: 10.1074/jbc.C109.094599 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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