5CQC

Crystal structure of the legionella pneumophila effector protein RavZ

5CQC の概要

• エントリーDOI: 10.2210/pdb5cqc/pdb
• 分子名称: putative RavZ protein, BARIUM ION (3 entities in total)
• 機能のキーワード: ulp-family cysteine protease, autophagy inhibitor, pi3p binding domain, legionella pneumophila effector protein, hydrolase
• 由来する生物種: Legionella pneumophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47256.24

構造登録者

Horenkamp, F.A.,Reinisch, K.M. (登録日: 2015-07-21, 公開日: 2015-09-09, 最終更新日: 2024-03-06)

主引用文献

Horenkamp, F.A.,Kauffman, K.J.,Kohler, L.J.,Sherwood, R.K.,Krueger, K.P.,Shteyn, V.,Roy, C.R.,Melia, T.J.,Reinisch, K.M.
The Legionella Anti-autophagy Effector RavZ Targets the Autophagosome via PI3P- and Curvature-Sensing Motifs.
Dev.Cell, 34:569-576, 2015

PubMed Abstract: Autophagy is a conserved membrane transport pathway used to destroy pathogenic microbes that access the cytosol of cells. The intracellular pathogen Legionella pneumophila interferes with autophagy by delivering an effector protein, RavZ, into the host cytosol. RavZ acts by cleaving membrane-conjugated Atg8/LC3 proteins from pre-autophagosomal structures. Its remarkable efficiency allows minute quantities of RavZ to block autophagy throughout the cell. To understand how RavZ targets pre-autophagosomes and specifically acts only on membrane-associated Atg8 proteins, we elucidated its structure. Revealed is a catalytic domain related in fold to Ulp family deubiquitinase-like enzymes and a C-terminal PI3P-binding module. RavZ targets the autophagosome via the PI3P-binding module and a catalytic domain helix, and it preferentially binds high-curvature membranes, intimating localization to highly curved domains in autophagosome intermediate membranes. RavZ-membrane interactions enhance substrate affinity, providing a mechanism for interfacial activation that also may be used by host autophagy proteins engaging only lipidated Atg8 proteins.

PubMed: 26343456
DOI: 10.1016/j.devcel.2015.08.010

実験手法

X-RAY DIFFRACTION (2.985 Å)