The E1-like enzymatic activity of the homodimeric ATG7 plays a pivotal role in driving the lipidation process of ATG8 orthologs (PMID: 10233150, 11096062, 11139573). Upon cleavage, ATG8 proteins undergo activation by ATG7 through adenylation, facilitated by MgATP. This process results in the formation of Atg8-acyl adenylate, which is subsequently attacked by the catalytic cysteine of Atg7, leading to the generation of a thiolester-bonded Atg7-Atg8 intermediate. A transthiolation reaction ensues, during which the C-terminus of Atg8 is transferred from Atg7's catalytic cysteine to that of the E2 enzyme, Atg3, creating a thiolester-linked Atg3-Atg8 conjugate (PMID: 17220875, 22055190). Ultimately, Atg8 is transferred from Atg3 to phosphatidylethanolamine (PE) with the help of E3 complex containing the Atg12-Atg5-ATG16L1 complex (PMID: 17986448). Additionally, ATG7 plays an important role in formation of E3 complex by activating ATG12 for its subsequent conjugation with ATG5. In this process, ATG12 undergoes adenylation by ATG7 and is then transferred to ATG5 via the involvement of the E2-like enzyme ATG10 (PMID: 9759731, 10508157, 22682742).
Experimental structure not availabe
Representations
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