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PDBsum entry 3rui
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References listed in PDB file
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Key reference
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Title
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Insights into noncanonical e1 enzyme activation from the structure of autophagic e1 atg7 with atg8.
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Authors
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S.B.Hong,
B.W.Kim,
K.E.Lee,
S.W.Kim,
H.Jeon,
J.Kim,
H.K.Song.
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Ref.
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Nat Struct Biol, 2011,
18,
1323-1330.
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PubMed id
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Abstract
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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. Here we present the structure of
the N-terminal domain of Atg7, revealing a unique protein fold and interactions
with both autophagic E2 enzymes Atg3 and Atg10. 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.
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