PDBsum entry 4r7e

Ligase

PDB id: 4r7e

Contents

Protein chain

69 a.a.

Metals

_ZN ×2

Waters ×9

References listed in PDB file

Key reference

• Title: Structure of the yeast bre1 ring domain.
• Authors: P.Kumar, C.Wolberger.
• Ref.: Proteins, 2015, 83, 1185-1190. [DOI no: 10.1002/prot.24812]
• PubMed id: 25864391

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. Proteins 2015; 83:1185-1190. © 2015 The Authors. Proteins: Structure, Function, and Bioinformatics Published by Wiley Periodicals, Inc.