General Information

ATG3 is an E2 conjugating enzyme required for the membrane association of ATG8 family proteins (PMID: 11100732, 11825910). It is responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly. The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). ATG3 forms an E1–E2 complex with ATG7 by forming a thioester bond cysteine of ATG3(PMID: 22055190). While only a portion of the human ATG3 protein has been crystallized in association with ATG12-ATG5-ATG16L1 (PMID: 24191030), insights from yeast ATG3 structures indicate a distinctive hammer-like shape for Atg3. This structure comprises a head and a handle. The head consist of a central six-stranded β-sheet (strands 1–6) enveloped by five α-helices. In contrast, the handle segment consists of a long α-helix (F) and a partially disordered loop region (PMID: 17227760).

Sequence 3D-Structure Experimental Structures

Monomer

Hetero-Oligomer

AlphaFold Structures