2KWQ
Mcm10 C-terminal DNA binding domain
Summary for 2KWQ
| Entry DOI | 10.2210/pdb2kwq/pdb |
| NMR Information | BMRB: 16872 |
| Descriptor | Protein MCM10 homolog, ZINC ION (2 entities in total) |
| Functional Keywords | mcm10, dna replication, dna binding, zinc motif, zinc ribbon, dna binding protein |
| Biological source | Xenopus laevis (clawed frog) |
| Total number of polymer chains | 1 |
| Total formula weight | 10727.31 |
| Authors | Robertson, P.D.,Chagot, B.,Chazin, W.J.,Eichman, B.F. (deposition date: 2010-04-15, release date: 2010-05-19, Last modification date: 2024-05-15) |
| Primary citation | Robertson, P.D.,Chagot, B.,Chazin, W.J.,Eichman, B.F. Solution NMR structure of the C-terminal DNA binding domain of Mcm10 reveals a conserved MCM motif. J.Biol.Chem., 285:22942-22949, 2010 Cited by PubMed Abstract: The eukaryotic DNA replication protein Mcm10 associates with chromatin in early S-phase and is required for assembly and function of the replication fork protein machinery. Xenopus laevis (X) Mcm10 binds DNA via a highly conserved internal domain (ID) and a C-terminal domain (CTD) that is unique to higher eukaryotes. Although the structural basis of the interactions of the ID with DNA and polymerase alpha is known, little information is available for the CTD. We have identified the minimal DNA binding region of the XMcm10-CTD and determined its three-dimensional structure by solution NMR. The CTD contains a globular domain composed of two zinc binding motifs. NMR chemical shift perturbation and mutational analysis show that ssDNA binds only to the N-terminal (CCCH-type) zinc motif, whose structure is unique to Mcm10. The second (CCCC-type) zinc motif is not involved in DNA binding. However, it is structurally similar to the CCCC zinc ribbon in the N-terminal oligomerization domain of eukaryotic and archaeal MCM helicases. NMR analysis of a construct spanning both the ID and CTD reveals that the two DNA binding domains are structurally independent in solution, supporting a modular architecture for vertebrate Mcm10. Our results provide insight in the action of Mcm10 in the replisome and support a model in which it serves as a central scaffold through coupling of interactions with partner proteins and the DNA. PubMed: 20489205DOI: 10.1074/jbc.M110.131276 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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