2LI5: NMR structure of Atg8-Atg7C30 complex

E1 enzymes activate ubiquitin-like proteins and transfer them to cognate E2 enzymes. Atg7, a noncanonical E1, activates two ubiquitin-like proteins, Atg8 and Atg12, and plays a crucial role in autophagy. Here, we report crystal structures of full-length Atg7 and its C-terminal domain bound to Atg8 and MgATP, as well as a solution structure of Atg8 bound to the extreme C-terminal domain (ECTD) of Atg7. The unique N-terminal domain (NTD) of Atg7 is responsible for Atg3 (E2) binding, whereas its C-terminal domain is comprised of a homodimeric adenylation domain (AD) and ECTD. The structural and biochemical data demonstrate that Atg8 is initially recognized by the C-terminal tail of ECTD and is then transferred to an AD, where the Atg8 C terminus is attacked by the catalytic cysteine to form a thioester bond. Atg8 is then transferred via a trans mechanism to the Atg3 bound to the NTD of the opposite protomer within a dimer.
PDB ID: 2LI5Download
MMDB ID: 94993
PDB Deposition Date: 2011/8/23
Updated in MMDB: 2011/11
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 2LI5: dimeric; determined by author
Molecular Components in 2LI5
Label Count Molecule
Proteins (2 molecules)
Autophagy-related Protein 8(Gene symbol: ATG8)
Molecule annotation
Ubiquitin-like Modifier-activating Enzyme Atg7(Gene symbol: ATG7)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB