3WAP
Crystal structure of Atg13 LIR-fused human LC3C_8-125
Summary for 3WAP
Entry DOI | 10.2210/pdb3wap/pdb |
Related | 3VTU 3VTV 3VTW 3WAL 3WAM 3WAN 3WAO |
Descriptor | Autophagy-related protein 13, Microtubule-associated proteins 1A/1B light chain 3C (1 entity in total) |
Functional Keywords | ubiquitin-like fold, autophagy, protein transport |
Biological source | Homo sapiens (human) More |
Cellular location | Cytoplasm, cytoskeleton : Q9BXW4 |
Total number of polymer chains | 1 |
Total formula weight | 15401.72 |
Authors | Suzuki, H.,Tabata, K.,Morita, E.,Kawasaki, M.,Kato, R.,Dobson, R.C.J.,Yoshimori, T.,Wakatsuki, S. (deposition date: 2013-05-06, release date: 2013-12-25, Last modification date: 2023-11-08) |
Primary citation | Suzuki, H.,Tabata, K.,Morita, E.,Kawasaki, M.,Kato, R.,Dobson, R.C.,Yoshimori, T.,Wakatsuki, S. Structural basis of the autophagy-related LC3/Atg13 LIR complex: recognition and interaction mechanism. Structure, 22:47-58, 2014 Cited by PubMed Abstract: Autophagy is a bulk degradation pathway that removes cytosolic materials to maintain cellular homeostasis. The autophagy-related gene 13 (Atg13) and microtubule associate protein 1 light chain 3 (LC3) proteins are required for autophagosome formation. We demonstrate that each of the human LC3 isoforms (LC3A, LC3B, and LC3C) interacts with Atg13 via the LC3 interacting region (LIR) of Atg13. Using X-ray crystallography, we solved the macromolecular structures of LC3A and LC3C, along with the complex structures of the LC3 isoforms with the Atg13 LIR. Together, our structural and binding analyses reveal that the side-chain of Lys49 of LC3 acts as a gatekeeper to regulate binding of the LIR. We verified this observation by mutation of Lys49 in LC3A, which significantly reduces LC3A positive puncta formation in cultured cells. Our results suggest that specific affinity of the LC3 isoforms to the Atg13 LIR is required for proper autophagosome formation. PubMed: 24290141DOI: 10.1016/j.str.2013.09.023 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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