Ontology highlight
ABSTRACT:
SUBMITTER: Taherbhoy AM
PROVIDER: S-EPMC3277881 | biostudies-literature | 2011 Nov
REPOSITORIES: biostudies-literature
Taherbhoy Asad M AM Tait Stephen W SW Kaiser Stephen E SE Williams Allison H AH Deng Alan A Nourse Amanda A Hammel Michal M Kurinov Igor I Rock Charles O CO Green Douglas R DR Schulman Brenda A BA
Molecular cell 20111101 3
Atg7 is a noncanonical, homodimeric E1 enzyme that interacts with the noncanonical E2 enzyme, Atg3, to mediate conjugation of the ubiquitin-like protein (UBL) Atg8 during autophagy. Here we report that the unique N-terminal domain of Atg7 (Atg7(NTD)) recruits a unique "flexible region" from Atg3 (Atg3(FR)). The structure of an Atg7(NTD)-Atg3(FR) complex reveals hydrophobic residues from Atg3 engaging a conserved groove in Atg7, important for Atg8 conjugation. We also report the structure of the ...[more]