The NMR structure of the autophagy-related protein Atg8
Autophagy is the process through which the bulk degradation of cytoplasmic components by the lysosomal/vacuolar system occurs in response to starvation conditions (Nakatogawa et al. 2009). In autophagy, a double-membrane structure called an autophagosome sequesters a portion of the cytoplasm and fuses with the lysosome/vacuole to deliver its contents into the organelle lumen. Recently, autophagy was found to have a crucial function in numerous biological processes including differentiation, antigen presentation and aging, and its dysfunction causes severe diseases such as neurodegeneration (Mizushima 2007).
Atg8 is a ubiquitin like protein, and plays an essential role for autophagosome formation in Saccharomyces cerevisiae. Atg8 is unique in that it is conjugated to the lipid phosphatidylethanolamine (PE) by a ubiquitin-like system, called the Atg8 system. In the Atg8 system, nascent Atg8 is cleaved at its C-terminal arginine residue by Atg4, a cysteine protease...
KeywordsClosed Conformation Autophagic Activity Aromatic Side Chain PreScission Protease Dihedral Angle Restraint
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