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Atg3 has an/-fold, and its core region is topologically similar to canonical E2 enzymes.
Atg3 has two regions inserted in the core region, one of which consists of80 residues and has a random coil structure in solution
and another with a long -helical structure that protrudes from the core region as far as 30A˚ . In vivo and in vitro analyses
suggested that the former region is responsible for binding Atg7, an E1-like enzyme, and that the latter is responsible for binding
Atg8.Asulfate ion was bound near the catalytic cysteine of Atg3, suggesting a possible binding site for the phosphate moiety of PE.

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2Â¥: Originally posted by ssssllllnnnn at 2014-11-19 02:07:12
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3Â¥2014-11-19 11:10:36
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