A novel conformation of the LC3-interacting region motif revealed by the structure of a complex between LC3B and RavZ

Do Hoon Kwon, Leehyeon Kim, Byeong Won Kim, Jun Hoe Kim, Kyung Hye Roh, Eui Ju Choi, Hyun Kyu Song

Research output: Contribution to journalArticle

6 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1093-1099
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume490
Issue number3
DOIs
Publication statusPublished - 2017 Aug 26

Keywords

  • Crystal structure
  • LC3
  • Legionella pneumophila
  • LIR motif
  • RavZ
  • Xenophagy

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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