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Uncovering the Structural Basis of a New Twist in Protein Ubiquitination

Author:
Puvar, Kedar, Luo, Zhao-Qing, Das, Chittaranjan
Source:
Trends in biochemical sciences 2019 v.44 no.5 pp. 467-477
ISSN:
0968-0004
Subject:
Legionella pneumophila, enzyme activity, enzymes, ubiquitin, ubiquitination, virulence
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.
Agid:
6233913