3VH1

Crystal structure of Saccharomyces cerevisiae Atg7 (1-595)

Summary for 3VH1

• Entry DOI: 10.2210/pdb3vh1/pdb
• Related: 3VH2 3VH3 3VH4
• Descriptor: Ubiquitin-like modifier-activating enzyme ATG7, ZINC ION (3 entities in total)
• Functional Keywords: autophagy, e1, zinc binding, metal binding protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Cytoplasm: P38862
• Total number of polymer chains: 1
• Total formula weight: 67881.82

Authors

Noda, N.N.,Satoo, K.,Inagaki, F. (deposition date: 2011-08-23, release date: 2011-09-21, Last modification date: 2024-03-20)

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

X-RAY DIFFRACTION (3 Å)