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Article

Structural and Biochemical Study of the Mono-ADP-Ribosyltransferase Domain of SdeA, a Ubiquitylating/Deubiquitylating Enzyme from Legionella pneumophila.

Journal of molecular biology - 17 Aug 2018

Kim Leehyeon, Kwon Do Hoon, Kim Bong Heon, Kim Jiyeon, Park Mi Rae, Park Zee-Yong, Song Hyun Kyu

Abstract excerpt

Conventional ubiquitylation occurs through an ATP-dependent three-enzyme cascade (E1, E2, and E3) that mediates the covalent conjugation of the C-terminus of ubiquitin to a lysine on the substrate. SdeA, which belongs to the SidE effector family of Legionella pneumophila, can transfer ubiquitin to endoplasmic reticulum-associated Rab-family GTPases in a manner independent of E1 and E2 enzymes. The novel...

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Identifiers

PMID: 29870726
DOI: 10.1016/j.jmb.2018.05.043

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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