3VX6

Crystal structure of Kluyveromyces marxianus Atg7NTD

Summary for 3VX6

• Entry DOI: 10.2210/pdb3vx6/pdb
• Related: 3VX7 3VX8
• Descriptor: E1 (2 entities in total)
• Functional Keywords: e2 binding, e1, ligase
• Biological source: Kluyveromyces marxianus
• Total number of polymer chains: 1
• Total formula weight: 32213.87

Authors

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. (deposition date: 2012-09-11, release date: 2012-11-14, Last modification date: 2023-11-08)

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

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: 23142983
DOI: 10.1038/nsmb.2451

Experimental method

X-RAY DIFFRACTION (2.6 Å)