Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8

Seung Beom Hong, Byeong Won Kim, Kyung Eun Lee, Se Woong Kim, Hyesung Jeon, Joon Kim, Hyun Kyu Song

Research output: Contribution to journalArticle

55 Citations (Scopus)

Abstract

Autophagy is the degradation of cellular organelles via the lysosomal pathway. The autophagic ubiquitin-like (Ubl) molecule Atg8 is activated by the E1-like enzyme Atg7. As this noncanonical E1 enzyme's domain organization is unique among Ubl-activating E1 enzymes, the structural basis for its interactions with Atg8 and partner E2 enzymes remains obscure. Here we present the structure of the N-terminal domain of Atg7, revealing a unique protein fold and interactions with both autophagic E2 enzymes Atg3 and Atg10. The structure of the C-terminal domain of Atg7 in complex with Atg8 shows the mode of dimerization and mechanism of recognition of Atg8. Notably, the catalytic cysteine residue in Atg7 is positioned close to the C-terminal glycine of Atg8, its target for thioester formation, potentially eliminating the need for large conformational rearrangements characteristic of other E1s.

Original languageEnglish
Pages (from-to)1323-1330
Number of pages8
JournalNature Structural and Molecular Biology
Volume18
Issue number12
DOIs
Publication statusPublished - 2011 Dec 1

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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