Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3WAP

Crystal structure of Atg13 LIR-fused human LC3C_8-125

Summary for 3WAP
Entry DOI10.2210/pdb3wap/pdb
Related3VTU 3VTV 3VTW 3WAL 3WAM 3WAN 3WAO
DescriptorAutophagy-related protein 13, Microtubule-associated proteins 1A/1B light chain 3C (1 entity in total)
Functional Keywordsubiquitin-like fold, autophagy, protein transport
Biological sourceHomo sapiens (human)
More
Cellular locationCytoplasm, cytoskeleton : Q9BXW4
Total number of polymer chains1
Total formula weight15401.72
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 citationSuzuki, 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: 24290141
DOI: 10.1016/j.str.2013.09.023
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

227111

數據於2024-11-06公開中

PDB statisticsPDBj update infoContact PDBjnumon