2LI5

NMR structure of Atg8-Atg7C30 complex

Summary for 2LI5

• Entry DOI: 10.2210/pdb2li5/pdb
• Related: 2KWC
• NMR Information: BMRB: 17879
• Descriptor: Autophagy-related protein 8, Ubiquitin-like modifier-activating enzyme ATG7 (2 entities in total)
• Functional Keywords: atg8, autophagy, ubiquitin like, protein transport
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Cytoplasmic vesicle, cvt vesicle membrane; Lipid-anchor: P38182; Cytoplasm: P38862
• Total number of polymer chains: 2
• Total formula weight: 17445.84

Authors

Kumeta, H.,Satoo, K.,Noda, N.N.,Fujioka, Y.,Ogura, K.,Nakatogawa, H.,Ohsumi, Y.,Inagaki, F. (deposition date: 2011-08-23, release date: 2011-11-16, Last modification date: 2024-05-15)

Primary citation

Noda, N.N.,Satoo, K.,Fujioka, Y.,Kumeta, H.,Ogura, K.,Nakatogawa, H.,Ohsumi, Y.,Inagaki, F.
Structural basis of Atg8 activation by a homodimeric E1, Atg7.
Mol.Cell, 44:462-475, 2011

PubMed Abstract: 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.

PubMed: 22055191
DOI: 10.1016/j.molcel.2011.08.035

Experimental method

SOLUTION NMR