5MSN
Structure of the Dcc1 Protein
5MSN の概要
| エントリーDOI | 10.2210/pdb5msn/pdb |
| 分子名称 | DCC1 protein (2 entities in total) |
| 機能のキーワード | winged-helix, dna repair, cell cycle |
| 由来する生物種 | Saccharomyces cerevisiae S288c |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 135163.64 |
| 構造登録者 | |
| 主引用文献 | Wade, B.O.,Liu, H.W.,Samora, C.P.,Uhlmann, F.,Singleton, M.R. Structural studies of RFC(C)(tf18) reveal a novel chromatin recruitment role for Dcc1. EMBO Rep., 18:558-568, 2017 Cited by PubMed Abstract: Replication factor C complexes load and unload processivity clamps from DNA and are involved in multiple DNA replication and repair pathways. The RFC variant complex is required for activation of the intra-S-phase checkpoint at stalled replication forks and aids the establishment of sister chromatid cohesion. Unlike other RFC complexes, RFC contains two non-Rfc subunits, Dcc1 and Ctf8. Here, we present the crystal structure of the Dcc1-Ctf8 heterodimer bound to the C-terminus of Ctf18. We find that the C-terminus of Dcc1 contains three-winged helix domains, which bind to both ssDNA and dsDNA We further show that these domains are required for full recruitment of the complex to chromatin, and correct activation of the replication checkpoint. These findings provide the first structural data on a eukaryotic seven-subunit clamp loader and define a new biochemical activity for Dcc1. PubMed: 28188145DOI: 10.15252/embr.201642825 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.002 Å) |
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