4R7E

Structure of Bre1 RING domain

Summary for 4R7E

Entry DOI	10.2210/pdb4r7e/pdb
Descriptor	E3 ubiquitin-protein ligase BRE1, ZINC ION (3 entities in total)
Functional Keywords	zinc finger domain, e3 ubiquitin ligase, monoubiquitination of histone h2b at k123, rad6, nucleosome, nucleus, ligase
Biological source	Saccharomyces cerevisiae (Baker's yeast)
Cellular location	Nucleus : Q07457
Total number of polymer chains	1
Total formula weight	8016.08
Authors	Kumar, P.,Wolberger, C. (deposition date: 2014-08-27, release date: 2015-05-13, Last modification date: 2024-02-28)
Primary citation	Kumar, P.,Wolberger, C. Structure of the yeast Bre1 RING domain. Proteins, 83:1185-1190, 2015 Cited by PubMed Abstract: 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. PubMed: 25864391 DOI: 10.1002/prot.24812 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.251 Å)

Structure validation