5IO3

Crystal structure of the legionella pneumophila effector protein RavZ - I422

5IO3 の概要

• エントリーDOI: 10.2210/pdb5io3/pdb
• 関連するPDBエントリー: 5HZY
• 分子名称: Uncharacterized protein RavZ (2 entities in total)
• 機能のキーワード: autophagy, atg8, deconjugating enzyme, protease, atg4b, hydrolase
• 由来する生物種: Legionella pneumophila subsp. pneumophila str. Philadelphia 1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56295.26

構造登録者

Kwon, D.H.,Kim, L.,Kim, B.-W.,Hong, S.B.,Song, H.K. (登録日: 2016-03-08, 公開日: 2016-11-09, 最終更新日: 2024-03-20)

主引用文献

Kwon, D.H.,Kim, S.,Jung, Y.O.,Roh, K.H.,Kim, L.,Kim, B.-W.,Hong, S.B.,Lee, I.Y.,Song, J.H.,Lee, W.C.,Choi, E.J.,Hwang, K.Y.,Song, H.K.
The 1:2 complex between RavZ and LC3 reveals a mechanism for deconjugation of LC3 on the phagophore membrane
Autophagy, 13:70-81, 2017

PubMed Abstract: Hosts utilize macroautophagy/autophagy to clear invading bacteria; however, bacteria have also developed a specific mechanism to survive by manipulating the host cell autophagy mechanism. One pathogen, Legionella pneumophila, can hinder host cell autophagy by using the specific effector protein RavZ that cleaves phosphatidylethanolamine-conjugated LC3 on the phagophore membrane. However, the detailed molecular mechanisms associated with the function of RavZ have hitherto remained unclear. Here, we report on the biochemical characteristics of the RavZ-LC3 interaction, the solution structure of the 1:2 complex between RavZ and LC3, and crystal structures of RavZ showing different conformations of the active site loop without LC3. Based on our biochemical, structural, and cell-based analyses of RavZ and LC3, both distant flexible N- and C-terminal regions containing LC3-interacting region (LIR) motifs are important for substrate recognition. These results suggest a novel mechanism of RavZ action on the phagophore membrane and lay the groundwork for understanding how bacterial pathogens can survive autophagy.

PubMed: 27791457
DOI: 10.1080/15548627.2016.1243199

実験手法

X-RAY DIFFRACTION (2.74 Å)