Ontology highlight
ABSTRACT:
SUBMITTER: Wu X
PROVIDER: S-EPMC10858943 | biostudies-literature | 2024 Feb
REPOSITORIES: biostudies-literature
Wu Xiangwei X Du Yunxiang Y Liang Lu-Jun LJ Ding Ruichao R Zhang Tianyi T Cai Hongyi H Tian Xiaolin X Pan Man M Liu Lei L
Nature communications 20240210 1
Ubiquitination, catalyzed usually by a three-enzyme cascade (E1, E2, E3), regulates various eukaryotic cellular processes. E3 ligases are the most critical components of this catalytic cascade, determining both substrate specificity and polyubiquitination linkage specificity. Here, we reveal the mechanism of a naturally occurring E3-independent ubiquitination reaction of a unique human E2 enzyme UBE2E1 by solving the structure of UBE2E1 in complex with substrate SETDB1-derived peptide. Guided by ...[more]