Autoinhibition Mechanism of the Ubiquitin-Conjugating Enzyme UBE2S by Autoubiquitination.
E2 enzyme
K11 chain
NMR
X-ray crystallography
cell cycle
enzyme mechanism
mass spectrometry
mitosis
molecular dynamics
ubiquitin
Journal
Structure (London, England : 1993)
ISSN: 1878-4186
Titre abrégé: Structure
Pays: United States
ID NLM: 101087697
Informations de publication
Date de publication:
06 08 2019
06 08 2019
Historique:
received:
08
03
2019
revised:
01
05
2019
accepted:
17
05
2019
pubmed:
25
6
2019
medline:
8
5
2020
entrez:
25
6
2019
Statut:
ppublish
Résumé
Ubiquitin-conjugating enzymes (E2s) govern key aspects of ubiquitin signaling. Emerging evidence suggests that the activities of E2s are modulated by posttranslational modifications; the structural underpinnings, however, are largely unclear. Here, we unravel the structural basis and mechanistic consequences of a conserved autoubiquitination event near the catalytic center of E2s, using the human anaphase-promoting complex/cyclosome-associated UBE2S as a model system. Crystal structures we determined of the catalytic ubiquitin carrier protein domain combined with MD simulations reveal that the active-site region is malleable, which permits an adjacent ubiquitin acceptor site, Lys
Identifiants
pubmed: 31230944
pii: S0969-2126(19)30170-4
doi: 10.1016/j.str.2019.05.008
pii:
doi:
Substances chimiques
Ubiquitin
0
Ube2S protein, human
EC 2.3.2.23
Ubiquitin-Conjugating Enzymes
EC 2.3.2.23
Lysine
K3Z4F929H6
Cysteine
K848JZ4886
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1195-1210.e7Commentaires et corrections
Type : CommentIn
Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.