Uncovering the Structural Basis of a New Twist in Protein Ubiquitination.
Trends Biochem Sci
; 44(5): 467-477, 2019 05.
Article
em En
| MEDLINE
| ID: mdl-30583962
ABSTRACT
Members of the SidE effector family from Legionella pneumophila represent a new paradigm in the ubiquitin world. These enzymes catalyze ubiquitination of target proteins via a mechanism different from that of conventional E1-E2-E3 biochemistry and play important roles in L. pneumophila virulence. They combine mono-ADP-ribosylation and phosphodiesterase activities to attach ubiquitin onto substrates, in great contrast to the orthodox pathway. A series of recent structural and mechanistic studies have clarified the action of these enzymes. Herein, we summarize the key insights into the structure and function of these proteins, emphasizing their modular nature, and discuss the biochemical implications of these proteins as well as areas of further exploration.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Legionella pneumophila
/
Proteínas de Membrana
Idioma:
En
Revista:
Trends Biochem Sci
Ano de publicação:
2019
Tipo de documento:
Article
País de afiliação:
Estados Unidos