7W75

Crystal structure of the K. lactis Bre1 RBD in complex with Rad6, crystal form I

Summary for 7W75

• Entry DOI: 10.2210/pdb7w75/pdb
• Descriptor: Ubiquitin-conjugating enzyme E2 2, E3 ubiquitin-protein ligase BRE1 (2 entities in total)
• Functional Keywords: complex, ubiquitin, ubiquitin ligase, gene regulation
• Biological source: Kluyveromyces lactis NRRL Y-1140; More
• Total number of polymer chains: 6
• Total formula weight: 130995.91

Authors

Shi, M.,Zhao, J.,Xiang, S. (deposition date: 2021-12-03, release date: 2023-03-29, Last modification date: 2024-10-23)

Primary citation

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

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

Experimental method

X-RAY DIFFRACTION (3.2 Å)