Summary information and primary citation

PDB-id
8t3y; SNAP-derived features in text and JSON formats; DNAproDB
Class
DNA binding protein-transferase-DNA
Method
cryo-EM (3.47 Å)
Summary
Structure of bre1-nucleosome complex - state1
Reference
Zhao F, Hicks CW, Wolberger C (2023): "Mechanism of histone H2B monoubiquitination by Bre1." Nat.Struct.Mol.Biol., 30, 1623-1627. doi: 10.1038/s41594-023-01137-x.
Abstract
Monoubiquitination of histone H2B-K120/123 plays several roles in regulating transcription, DNA replication and the DNA damage response. The structure of a nucleosome in complex with the dimeric RING E3 ligase Bre1 reveals that one RING domain binds to the nucleosome acidic patch, where it can position the E2 ubiquitin conjugating enzyme Rad6, while the other RING domain contacts the DNA. Comparisons with H2A-specific E3 ligases suggest a general mechanism of tuning histone specificity via the non-E2-binding RING domain.

Cartoon-block schematics in six views (download the tarball)

PyMOL session file Download PDB file View in 3Dmol.js