A Ca2+-regulated deAMPylation switch in human and bacterial FIC proteins
In many AMPylating FIC proteins a structurally conserved glutamate represses AMPylation. Here, the authors show that this glutamate supports deAMPylation in Enterococcus faecalis FIC (EfFIC), and that EfFIC switches from AMPylation to deAMPylation by binding Ca2+ at distinct sites.
Enregistré dans:
Auteurs principaux: | Simon Veyron, Giulia Oliva, Monica Rolando, Carmen Buchrieser, Gérald Peyroche, Jacqueline Cherfils |
---|---|
Format: | article |
Langue: | EN |
Publié: |
Nature Portfolio
2019
|
Sujets: | |
Accès en ligne: | https://doaj.org/article/c82bc1c01f6d4d08a41f42155b940323 |
Tags: |
Ajouter un tag
Pas de tags, Soyez le premier à ajouter un tag!
|
Documents similaires
-
Structures of a deAMPylation complex rationalise the switch between antagonistic catalytic activities of FICD
par: Luke A. Perera, et autres
Publié: (2021) -
FICD activity and AMPylation remodelling modulate human neurogenesis
par: Pavel Kielkowski, et autres
Publié: (2020) -
A Unique <italic toggle="yes">cis</italic>-Encoded Small Noncoding RNA Is Regulating <italic toggle="yes">Legionella pneumophila</italic> Hfq Expression in a Life Cycle-Dependent Manner
par: Giulia Oliva, et autres
Publié: (2017) -
Specificity of AMPylation of the human chaperone BiP is mediated by TPR motifs of FICD
par: Joel Fauser, et autres
Publié: (2021) -
Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1
par: Jiqing Du, et autres
Publié: (2021)