This entry represents a group of ubiquitin-like-conjugating enzymes, including Atg3 and Atg10.Atg3 is the E2 enzyme for the LC3 lipidation process []. It is essential for autophagocytosis. The super protein complex, the Atg16L complex, consists of multiple Atg12-Atg5 conjugates. Atg16L has an E3-like role in the LC3 lipidation reaction. The activated intermediate, LC3-Atg3 (E2), is recruited to the site where the lipidation takes place []. Atg3 catalyses the conjugation of Atg8 and phosphatidylethanolamine (PE). Atg3 has an alpha/β-fold, and its core region is topologically similar to canonical E2 enzymes. Atg3 has two regions inserted in the core region and another with a long α-helical structure that protrudes from the core region as far as 30 A []. It interacts with atg8 through an intermediate thioester bond between Cys-288 and the C-terminal Gly of atg8. It also interacts with the C-terminal region of the E1-like atg7 enzyme.Atg10 acts as an E2-like enzyme that catalyzes the conjugation of ATG12 to ATG5 [].
This superfamily represents the second subdomain found in the N-terminal domain of ubiquitin-like modifier-activating enzyme Atg7. In Arabidopsis, the N-terminal domain binds the E2 enzymes Atg10 and Atg3 [].
This superfamily represents the first subdomain found in the N-terminal domain of ubiquitin-like modifier-activating enzyme Atg7. In Arabidopsis, the N-terminal domain binds the E2 enzymes Atg10 and Atg3 [].
