8T3W

Structure of Bre1-nucleosome complex - state2

Summary for 8T3W

• Entry DOI: 10.2210/pdb8t3w/pdb
• EMDB information: 41015
• Descriptor: Histone H3.2, Histone H4, Histone H2A type 1, ... (8 entities in total)
• Functional Keywords: h2b ubiquitin, nucleosome acidic patch binding protein, dna binding protein-transferase-dna complex, dna binding protein/transferase/dna
• Biological source: Xenopus laevis (African clawed frog); More
• Total number of polymer chains: 12
• Total formula weight: 223800.65

Authors

Zhao, F.,Hicks, C.W.,Wolberger, C. (deposition date: 2023-06-07, release date: 2023-10-18, Last modification date: 2023-11-22)

Primary citation

Zhao, F.,Hicks, C.W.,Wolberger, C.
Mechanism of histone H2B monoubiquitination by Bre1.
Nat.Struct.Mol.Biol., 30:1623-1627, 2023

PubMed 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.

PubMed: 37872231
DOI: 10.1038/s41594-023-01137-x

Experimental method

ELECTRON MICROSCOPY (3.25 Å)