A novel conformation of the LC3-interacting region motif revealed by the structure of a complex between LC3B and RavZ
- Authors
- Kwon, Do Hoon; Kim, Leehyeon; Kim, Byeong-Won; Kim, Jun Hoe; Roh, Kyung-Hye; Choi, Eui-Ju; Song, Hyun Kyu
- Issue Date
- 26-Aug-2017
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- Crystal structure; LC3; LIR motif; Legionella pneumophila; RavZ; Xenophagy
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.490, no.3, pp.1093 - 1099
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 490
- Number
- 3
- Start Page
- 1093
- End Page
- 1099
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/82524
- DOI
- 10.1016/j.bbrc.2017.06.173
- ISSN
- 0006-291X
- 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 (3-sheet conformation and thus provide specific ionic interactions with LOB 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. (C) 2017 Elsevier Inc. All rights reserved.
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Collections - Graduate School > Department of Life Sciences > 1. Journal Articles
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