Molecular Basis of Ubiquitination Catalyzed by the Bacterial Transglutaminase MavC.

ABSTRACT: The Legionella pneumophila effector MavC is a transglutaminase that carries out atypical ubiquitination of the host ubiquitin (Ub)-conjugation enzyme UBE2N by catalyzing the formation of an isopeptide bond between Gln40_Ub and Lys92_UBE2N, which leads to inhibition of signaling in the NF-κB pathway. In the absence of UBE2N, MavC deamidates Ub at Gln40 or catalyzes self-ubiquitination. However, the mechanisms underlying these enzymatic activities of MavC are poorly understood at the molecular level. This study reports the structure of the MavC-UBE2N-Ub ternary complex representing a snapshot of MavC-catalyzed crosslinking of UBE2N and Ub, which reveals the way by which UBE2N-Ub binds to the Insertion and Tail domains of MavC. Based on the structural and experiment

SUBMITTER: Guan H 

PROVIDER: S-EPMC7312448 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature