2KWU
Solution Structure of UBM2 of murine Polymerase iota in Complex with Ubiquitin
2KWU の概要
| エントリーDOI | 10.2210/pdb2kwu/pdb |
| 関連するPDBエントリー | 2KHU 2KHW |
| NMR情報 | BMRB: 16880 |
| 分子名称 | DNA polymerase iota, Ubiquitin (2 entities in total) |
| 機能のキーワード | polymerase iota, ubiquitin, ubiquitin-binding motif, ubm, tls, protein binding-signaling protein complex, protein binding/signaling protein |
| 由来する生物種 | Mus musculus (mouse) 詳細 |
| 細胞内の位置 | Nucleus (By similarity): Q6R3M4 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 14281.08 |
| 構造登録者 | Burschowsky, D.,Rudolf, F.,Rabut, G.,Herrmann, T.,Peter, M.,Wider, G. (登録日: 2010-04-19, 公開日: 2010-10-06, 最終更新日: 2024-05-01) |
| 主引用文献 | Burschowsky, D.,Rudolf, F.,Rabut, G.,Herrmann, T.,Matthias, P.,Wider, G. Structural analysis of the conserved ubiquitin-binding motifs (UBMs) of the translesion polymerase iota in complex with ubiquitin. J.Biol.Chem., 286:1364-1373, 2011 Cited by PubMed Abstract: Ubiquitin-binding domains (UBDs) provide specificity to the ubiquitin system, which is also involved in translesion synthesis (TLS) in eukaryotic cells. Upon DNA damage, the UBDs (UBM domains) of polymerase iota (Pol ι) interact with ubiquitinated proliferating cell nuclear antigen to regulate the interchange between processive DNA polymerases and TLS. We report a biophysical analysis and solution structures of the two conserved UBM domains located in the C-terminal tail of murine Pol ι in complex with ubiquitin. The 35-amino acid core folds into a helix-turn-helix motif, which belongs to a novel domain fold. Similar to other UBDs, UBMs bind to ubiquitin on the hydrophobic surface delineated by Leu-8, Ile-44, and Val-70, however, slightly shifted toward the C terminus. In addition, UBMs also use electrostatic interactions to stabilize binding. NMR and fluorescence spectroscopy measurements revealed that UBMs bind monoubiquitin, and Lys-63- but not Lys-48-linked chains. Importantly, these biophysical data are supported by functional studies. Indeed, yeast cells expressing ubiquitin mutants specifically defective for UBM binding are viable but sensitive to DNA damaging conditions that require TLS for repair. PubMed: 20929865DOI: 10.1074/jbc.M110.135038 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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