3RUI: Crystal Structure Of Atg7c-atg8 Complex

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.
PDB ID: 3RUIDownload
MMDB ID: 95221
PDB Deposition Date: 2011/5/5
Updated in MMDB: 2011/11
Experimental Method:
x-ray diffraction
Resolution: 1.91  Å
Source Organism:
Similar Structures:
Biological Unit for 3RUI: tetrameric; determined by author and by software (PISA)
Molecular Components in 3RUI
Label Count Molecule
Proteins (4 molecules)
Ubiquitin-like Modifier-activating Enzyme Atg7(Gene symbol: ATG7)
Molecule annotation
Autophagy-related Protein 8(Gene symbol: ATG8)
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB