Abstract：
: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 homodimeric Atg7 C-terminal domain, which is homologous to canonical E1s and bacterial antecedents. The structures, SAXS, and crosslinking data allow modeling of a full-length, dimeric (Atg7~Atg8-Atg3)(2) complex. The model and biochemical data provide a rationale for Atg7 dimerization: Atg8 is transferred in trans from the catalytic cysteine of one Atg7 protomer to Atg3 bound to the N-terminal domain of the opposite Atg7 protomer within the homodimer. The studies reveal a distinctive E1~UBL-E2 architecture for enzymes mediating autophagy.
journal_name
Mol Celljournal_title
Molecular cellauthors
Taherbhoy AM,Tait SW,Kaiser SE,Williams AH,Deng A,Nourse A,Hammel M,Kurinov I,Rock CO,Green DR,Schulman BAdoi
10.1016/j.molcel.2011.08.034subject
Has Abstractpub_date
2011-11-04 00:00:00pages
451-61issue
3eissn
1097-2765issn
1097-4164pii
S1097-2765(11)00767-2journal_volume
44pub_type
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