7EU4
Crystal structure of plant ATG12 complexed with the AIM12 of ATG3
Summary for 7EU4
| Entry DOI | 10.2210/pdb7eu4/pdb |
| Descriptor | Ubiquitin-like protein ATG12B, AIM12 from Autophagy-related protein 3 (2 entities in total) |
| Functional Keywords | autophagy, ubiquitin-like modifier, e2, plant protein |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) More |
| Total number of polymer chains | 18 |
| Total formula weight | 152738.00 |
| Authors | Matoba, K.,Noda, N.N. (deposition date: 2021-05-16, release date: 2021-07-28, Last modification date: 2023-11-29) |
| Primary citation | Matoba, K.,Noda, N.N. Atg12-Interacting Motif Is Crucial for E2-E3 Interaction in Plant Atg8 System. Biol.Pharm.Bull., 44:1337-1343, 2021 Cited by PubMed Abstract: Autophagy is an intracellular degradation system regulating cellular homeostasis. The two ubiquitin-like modification systems named the Atg8 system and the Atg12 system are essential for autophagy. Atg8 and Atg12 are ubiquitin-like proteins covalently conjugated with a phosphatidylethanolamine (PE) and Atg5, respectively, via enzymatic reactions. The Atg8-PE conjugate binds to autophagic membranes and recruits various proteins through direct interaction, whereas the Atg12-Atg5 conjugate recognizes Atg3, the E2 enzyme for Atg8, and facilitates Atg8-PE conjugation by functioning as the E3 enzyme. Although structural and biochemical analyses have well established the Atg8-family interacting motif (AIM), studies on the interacting sequence for Atg12 are rare (only one example for human ATG12-ATG3), thereby making it challenging to define a binding motif. Here we determined the crystal structure of the plant ATG12b as a complex with the ATG12b-binding region of ATG3 and revealed that ATG12b recognizes the aspartic acid (Asp)-methionine (Met) motif in ATG3 via a hydrophobic pocket and a basic residue, which we confirmed critical for the complex formation by mutational analysis. This recognition mode is similar to that reported between human ATG12 and ATG3, suggesting that the Asp-Met sequence is a conserved Atg12-interacting motif (AIM12). These data suggest that AIM12 mediates E2-E3 interaction during Atg8 lipidation and provide structural basis for developing chemicals that regulate autophagy by targeting Atg12-family proteins. PubMed: 34193767DOI: 10.1248/bpb.b21-00439 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
Download full validation report
