2dym
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The crystal structure of Saccharomyces cerevisiae Atg5- Atg16(1-46) complex
OverviewOverview
Atg5 is covalently modified with a ubiquitin-like modifier, Atg12, and the, Atg12-Atg5 conjugate further forms a complex with the multimeric protein, Atg16. The Atg12-Atg5.Atg16 multimeric complex plays an essential role in, autophagy, the bulk degradation system conserved in all eukaryotes. We, have reported here the crystal structure of Atg5 complexed with the, N-terminal region of Atg16 at 1.97A resolution. Atg5 comprises two, ubiquitin-like domains that flank a helix-rich domain. The N-terminal, region of Atg16 has a helical structure and is bound to the groove formed, by these three domains. In vitro analysis showed that Arg-35 and Phe-46 of, Atg16 are crucial for the interaction. Atg16, with a mutation at these, residues, failed to localize to the pre-autophagosomal structure and could, not restore autophagy in Atg16-deficient yeast strains. Furthermore, these, Atg16 mutants could not restore a severe reduction in the formation of the, Atg8-phosphatidylethanolamine conjugate, another essential factor for, autophagy, in Atg16-deficient strains under starvation conditions. These, results taken together suggest that the direct interaction between Atg5, and Atg16 is crucial to the performance of their roles in autophagy.
About this StructureAbout this Structure
2DYM is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Structure of Atg5.Atg16, a complex essential for autophagy., Matsushita M, Suzuki NN, Obara K, Fujioka Y, Ohsumi Y, Inagaki F, J Biol Chem. 2007 Mar 2;282(9):6763-72. Epub 2006 Dec 27. PMID:17192262
Page seeded by OCA on Wed Jan 23 14:37:23 2008