▶Subject: Structure of autophagic enzymes for autophagosome formation

▶Speaker: Professor. Hyun Kyu Song (Department of Life Sciences, Korea University)

▶Date: 4:00PM/September/13(Fri)/2013
 

▶Place: Auditorium(1F),Postech Biotech Center

*Abctract

Autophagy is the degradation of cellular organelles via the lysosomal pathway. The autophagic ubiquitin-like (Ubl) molecule Atg8 is activated by the E1-like enzyme Atg7. As this noncanonical E1 enzyme’s domain organization is unique among Ubl-activating E1 enzymes, the structural basis for its interactions with Atg8 and partner E2 enzymes remains obscure.
The structure of the C-terminal domain of Atg7 in complex with Atg8 shows the mode of dimerization and mechanism of recognition of Atg8.
Notably, the catalytic cysteine residue in Atg7 is positioned close to the C-terminal glycine of Atg8, its target for thioester formation, potentially eliminating the need for large conformational rearrangements characteristic of other E1s.
The structure of the N-terminal domain of Atg7 reveals a unique protein fold and interactions with both autophagic E2 enzymes Atg3 and Atg10. Here I also present the structure of Atg10 from
S. cerevisiae at 2.7 ? resolution. The core-folding of Atg10 is well conserved with that of Atg3, however two unique features in the structure of Atg10 are identified. Current structures of autophagic E1- and E2-enzyme provide a framework for understanding autophagosome formation in autophagy.

▶Inquiry: Prof. Cheol-Sang Hwang(279-2352)