3VX8
Crystal structure of Arabidopsis thaliana Atg7NTD-Atg3 complex
Summary for 3VX8
| Entry DOI | 10.2210/pdb3vx8/pdb |
| Related | 3VX6 3VX7 |
| Descriptor | Ubiquitin-like modifier-activating enzyme atg7, Autophagy-related protein 3 (3 entities in total) |
| Functional Keywords | e1-e2 complex, ligase |
| Biological source | Arabidopsis thaliana (mouse-ear cress) More |
| Cellular location | Cytoplasm (Probable): Q0WWQ1 |
| Total number of polymer chains | 4 |
| Total formula weight | 138046.51 |
| Authors | Matoba, K.,Fujioka, Y.,Noda, N.N. (deposition date: 2012-09-11, release date: 2012-11-14, Last modification date: 2023-10-18) |
| Primary citation | Yamaguchi, M.,Matoba, K.,Sawada, R.,Fujioka, Y.,Nakatogawa, H.,Yamamoto, H.,Kobashigawa, Y.,Hoshida, H.,Akada, R.,Ohsumi, Y.,Noda, N.N.,Inagaki, F. Noncanonical recognition and UBL loading of distinct E2s by autophagy-essential Atg7. Nat.Struct.Mol.Biol., 19:1250-1256, 2012 Cited by PubMed Abstract: Autophagy requires ubiquitin-like Atg8 and Atg12 conjugation systems, where Atg7 has a critical role as the sole E1 enzyme. Although Atg7 recognizes two distinct E2s, Atg3 and Atg10, it is not understood how Atg7 correctly loads these E2s with their cognate ubiquitin-like proteins, Atg8 and Atg12. Here, we report the crystal structures of the N-terminal domain of Atg7 bound to Atg10 or Atg3 of thermotolerant yeast and plant homologs. The observed Atg7-Atg10 and Atg7-Atg3 interactions, which resemble each other but are quite distinct from the canonical E1-E2 interaction, makes Atg7 suitable for transferring Atg12 to Atg10 and Atg8 to Atg3 by a trans mechanism. Notably, in vitro experiments showed that Atg7 loads Atg3 and Atg10 with Atg8 and Atg12 in a nonspecific manner, which suggests that cognate conjugate formation in vivo is not an intrinsic quality of Atg7. PubMed: 23142983DOI: 10.1038/nsmb.2451 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.11 Å) |
Structure validation
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