4R7E: Structure Of Bre1 Ring Domain

Monoubiquitination of histone H2B at Lys123 in yeast plays a critical role in regulating transcription, mRNA export, DNA replication, and the DNA damage response. The RING E3 ligase, Bre1, catalyzes monoubiquitination of H2B in concert with the E2 ubiquitin-conjugating enzyme, Rad6. The crystal structure of a C-terminal fragment of Bre1 shows that the catalytic RING domain is preceded by an N-terminal helix that mediates coiled-coil interactions with a crystallographically related monomer. Homology modeling suggests that the human homologue of Bre1, RNF20/RNF40, heterodimerizes through similar coiled-coil interactions.
PDB ID: 4R7EDownload
MMDB ID: 129218
PDB Deposition Date: 2014/8/27
Updated in MMDB: 2015/08
Experimental Method:
x-ray diffraction
Resolution: 2.25  Å
Source Organism:
Similar Structures:
Biological Unit for 4R7E: dimeric; determined by author and by software (PISA)
Molecular Components in 4R7E
Label Count Molecule
Proteins (2 molecules)
E3 Ubiquitin-protein Ligase Bre1(Gene symbol: BRE1)
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB