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http://purl.uniprot.org/citations/17192262http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17192262http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17192262http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/17192262http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m609876200"xsd:string
http://purl.uniprot.org/citations/17192262http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m609876200"xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/author"Inagaki F."xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/author"Inagaki F."xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/author"Matsushita M."xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/author"Matsushita M."xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/author"Obara K."xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/author"Obara K."xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/author"Fujioka Y."xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/author"Fujioka Y."xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/author"Ohsumi Y."xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/author"Ohsumi Y."xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/author"Suzuki N.N."xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/author"Suzuki N.N."xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/pages"6763-6772"xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/pages"6763-6772"xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/title"Structure of Atg5.Atg16, a complex essential for autophagy."xsd:string
http://purl.uniprot.org/citations/17192262http://purl.uniprot.org/core/title"Structure of Atg5.Atg16, a complex essential for autophagy."xsd:string