Insights into catalysis and function of phosphoribosyl-linked serine ubiquitination.

ABSTRACT: Conventional ubiquitination regulates key cellular processes by catalysing the ATP-dependent formation of an isopeptide bond between ubiquitin (Ub) and primary amines in substrate proteins ¹ . Recently, the SidE family of bacterial effector proteins (SdeA, SdeB, SdeC and SidE) from pathogenic Legionella pneumophila were shown to use NAD⁺ to mediate phosphoribosyl-linked ubiquitination of serine residues in host proteins^{2, 3}. However, the molecular architecture of the catalytic platform that enables this complex multistep process remains unknown. Here we describe the structure of the catalytic core of SdeA, comprising mono-ADP-ribosyltransferase (mART) and phosphodiesterase (PDE) domains, and shed light on the activity of two distinct catalytic sites for ser

SUBMITTER: Kalayil S 

PROVIDER: S-EPMC5980784 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature