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PDBsum entry 4gdk
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Protein binding
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PDB id
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4gdk
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Contents |
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88 a.a.
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267 a.a.
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34 a.a.
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35 a.a.
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References listed in PDB file
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Key reference
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Title
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Structure of the human atg12~atg5 conjugate required for lc3 lipidation in autophagy.
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Authors
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C.Otomo,
Z.Metlagel,
G.Takaesu,
T.Otomo.
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Ref.
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Nat Struct Biol, 2013,
20,
59-66.
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PubMed id
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Abstract
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The autophagy factor ATG12~ATG5 conjugate exhibits E3 ligase-like activity which
facilitates the lipidation of members of the LC3 family. The crystal structure
of the human ATG12~ATG5 conjugate bound to the N-terminal region of ATG16L1, the
factor that recruits the conjugate to autophagosomal membranes, reveals an
integrated architecture in which ATG12 docks onto ATG5 through conserved
residues. ATG12 and ATG5 are oriented such that other conserved residues on each
molecule, including the conjugation junction, form a continuous surface patch.
Mutagenesis data support the importance of both the interface between ATG12 and
ATG5 and the continuous patch for E3 activity. The ATG12~ATG5 conjugate
interacts with the E2 enzyme ATG3 with high affinity through another surface
location that is exclusive to ATG12, suggesting a different role of the
continuous patch in E3 activity. These findings provide a foundation for
understanding the mechanism of LC3 lipidation.
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