4R7E

Structure of Bre1 RING domain

4R7E の概要

• エントリーDOI: 10.2210/pdb4r7e/pdb
• 分子名称: E3 ubiquitin-protein ligase BRE1, ZINC ION (3 entities in total)
• 機能のキーワード: zinc finger domain, e3 ubiquitin ligase, monoubiquitination of histone h2b at k123, rad6, nucleosome, nucleus, ligase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Nucleus : Q07457
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8016.08

構造登録者

Kumar, P.,Wolberger, C. (登録日: 2014-08-27, 公開日: 2015-05-13, 最終更新日: 2024-02-28)

主引用文献

Kumar, P.,Wolberger, C.
Structure of the yeast Bre1 RING domain.
Proteins, 83:1185-1190, 2015

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

実験手法

X-RAY DIFFRACTION (2.251 Å)