8T3Y

Structure of Bre1-nucleosome complex - state1

Summary for 8T3Y

Entry DOI	10.2210/pdb8t3y/pdb
EMDB information	41016
Descriptor	Histone H3.2, Histone H4, Histone H2A type 1, ... (8 entities in total)
Functional Keywords	h2b ubiquitin e3 ligase, dimer, 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: 2023-06-08, 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 Cited by 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 PDB entries with the same primary citation
Experimental method	ELECTRON MICROSCOPY (3.47 Å)

Structure validation