Mechanism of phosphoribosyl-ubiquitination mediated by a single Legionella effector.

ABSTRACT: Ubiquitination is a post-translational modification that regulates many cellular processes in eukaryotes^1-4. The conventional ubiquitination cascade culminates in a covalent linkage between the C terminus of ubiquitin (Ub) and a target protein, usually on a lysine side chain^1,5. Recent studies of the Legionella pneumophila SidE family of effector proteins revealed a ubiquitination method in which a phosphoribosyl ubiquitin (PR-Ub) is conjugated to a serine residue on substrates via a phosphodiester bond^6-8. Here we present the crystal structure of a fragment of the SidE family member SdeA that retains ubiquitination activity, and determine the mechanism of this unique post-translational modification. The structure reveals that the catalytic module contains

SUBMITTER: Akturk A 

PROVIDER: S-EPMC5980775 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature