7W75
Crystal structure of the K. lactis Bre1 RBD in complex with Rad6, crystal form I
7W75 の概要
エントリーDOI | 10.2210/pdb7w75/pdb |
分子名称 | Ubiquitin-conjugating enzyme E2 2, E3 ubiquitin-protein ligase BRE1 (2 entities in total) |
機能のキーワード | complex, ubiquitin, ubiquitin ligase, gene regulation |
由来する生物種 | Kluyveromyces lactis NRRL Y-1140 詳細 |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 130995.91 |
構造登録者 | |
主引用文献 | Shi, M.,Zhao, J.,Zhang, S.,Huang, W.,Li, M.,Bai, X.,Zhang, W.,Zhang, K.,Chen, X.,Xiang, S. Structural basis for the Rad6 activation by the Bre1 N-terminal domain. Elife, 12:-, 2023 Cited by PubMed Abstract: The mono-ubiquitination of the histone protein H2B (H2Bub1) is a highly conserved histone post-translational modification that plays critical roles in many fundamental processes. In yeast, this modification is catalyzed by the conserved Bre1-Rad6 complex. Bre1 contains a unique N-terminal Rad6-binding domain (RBD), how it interacts with Rad6 and contributes to the H2Bub1 catalysis is unclear. Here, we present crystal structure of the Bre1 RBD-Rad6 complex and structure-guided functional studies. Our structure provides a detailed picture of the interaction between the dimeric Bre1 RBD and a single Rad6 molecule. We further found that the interaction stimulates Rad6's enzymatic activity by allosterically increasing its active site accessibility and likely contribute to the H2Bub1 catalysis through additional mechanisms. In line with these important functions, we found that the interaction is crucial for multiple H2Bub1-regulated processes. Our study provides molecular insights into the H2Bub1 catalysis. PubMed: 36912886DOI: 10.7554/eLife.84157 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.2 Å) |
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