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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DOI10.2210/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
Shi, M.,Zhao, J.,Xiang, S. (登録日: 2021-12-03, 公開日: 2023-03-29, 最終更新日: 2024-10-23)
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: 36912886
DOI: 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)
構造検証レポート
Validation report summary of 7w75
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-16に公開中

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