2KWQ

Mcm10 C-terminal DNA binding domain

2KWQ の概要

• エントリーDOI: 10.2210/pdb2kwq/pdb
• NMR情報: BMRB: 16872
• 分子名称: Protein MCM10 homolog, ZINC ION (2 entities in total)
• 機能のキーワード: mcm10, dna replication, dna binding, zinc motif, zinc ribbon, dna binding protein
• 由来する生物種: Xenopus laevis (clawed frog)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10727.31

構造登録者

Robertson, P.D.,Chagot, B.,Chazin, W.J.,Eichman, B.F. (登録日: 2010-04-15, 公開日: 2010-05-19, 最終更新日: 2024-05-15)

主引用文献

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

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: 20489205
DOI: 10.1074/jbc.M110.131276

実験手法

SOLUTION NMR