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5XAD

NLIR - LC3B fusion protein

Summary for 5XAD
Entry DOI10.2210/pdb5xad/pdb
Related5XAC 5XAE
DescriptorMicrotubule-associated proteins 1A/1B light chain 3B, Uncharacterised protein (3 entities in total)
Functional Keywordsautophagy, lc3, atg8, fusion protein, protein binding
Biological sourceHomo sapiens (Human)
More
Cellular locationCytoplasm, cytoskeleton: Q9GZQ8
Total number of polymer chains4
Total formula weight33667.92
Authors
Kwon, D.H.,Kim, L.,Song, H.K. (deposition date: 2017-03-12, release date: 2017-07-12, Last modification date: 2023-11-22)
Primary citationKwon, D.H.,Kim, L.,Kim, B.W.,Kim, J.H.,Roh, K.H.,Choi, E.J.,Song, H.K.
A novel conformation of the LC3-interacting region motif revealed by the structure of a complex between LC3B and RavZ
Biochem. Biophys. Res. Commun., 490:1093-1099, 2017
Cited by
PubMed Abstract: LC3-family member proteins play a critical role in autophagy, a cellular process responsible for the degradation of massive cellular components including intracellular pathogens. A variety of molecules involved in the autophagic pathway engage in specific interactions with a unique sequence motif referred to as the LIR (LC3-interacting region) motif. Although identification of conserved structural features of LIR motifs in complex with LC3-family members has established a canonical LIR motif, atypical conformations of LIR motifs have recently been revealed. Here, we determined the three-dimensional crystal structures of LC3B in complex with three different LIR motifs of RavZ from Legionella pneumophila, an intracellular pathogen that can manipulate the host autophagy system. The tandem LIR motifs located in the N-terminal region of RavZ adopt a novel β-sheet conformation and thus provide specific ionic interactions with LC3B in addition to canonical hydrophobic plugged-in interactions. Consequently, these motifs possess higher binding affinity to LC3-family members than canonical LIR motifs, although the tandem repeats can only bind to one LC3 molecule. These findings broaden our understanding of the functional repertoire of LIR motifs in autophagy.
PubMed: 28668392
DOI: 10.1016/j.bbrc.2017.06.173
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.88 Å)
Structure validation

238582

數據於2025-07-09公開中

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