5NNY

Crystal structure of the phosphatase domain from the Legionella effector WipB

5NNY の概要

• エントリーDOI: 10.2210/pdb5nny/pdb
• 分子名称: WipB (2 entities in total)
• 機能のキーワード: legionella effector, serine/threonine phosphatase, phosphoesterase fold, hydrolase
• 由来する生物種: Legionella pneumophila
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72674.62

構造登録者

Pinotsis, N.,Waksman, G.,Prevost, M.S. (登録日: 2017-04-10, 公開日: 2017-09-06, 最終更新日: 2024-01-17)

主引用文献

Prevost, M.S.,Pinotsis, N.,Dumoux, M.,Hayward, R.D.,Waksman, G.
The Legionella effector WipB is a translocated Ser/Thr phosphatase that targets the host lysosomal nutrient sensing machinery.
Sci Rep, 7:9450-9450, 2017

PubMed Abstract: Legionella pneumophila infects human alveolar macrophages and is responsible for Legionnaire's disease, a severe form of pneumonia. L. pneumophila encodes more than 300 putative effectors, which are translocated into the host cell via the Dot/Icm type IV secretion system. These effectors highjack the host's cellular processes to allow bacterial intracellular growth and replication. Here we adopted a multidisciplinary approach to investigate WipB, a Dot/Icm effector of unknown function. The crystal structure of the N-terminal domain at 1.7 Å resolution comprising residues 25 to 344 revealed that WipB harbours a Ser/Thr phosphatase domain related to the eukaryotic phospho-protein phosphatase (PPP) family. The C-terminal domain (residues 365-524) is sufficient to pilot the effector to acidified LAMP1-positive lysosomal compartments, where WipB interacts with the v-ATPase and the associated LAMTOR1 phosphoprotein, key components of the lysosomal nutrient sensing (LYNUS) apparatus that controls the mammalian target of rapamycin (mTORC1) kinase complex at the lysosomal surface. We propose that WipB is a lysosome-targeted phosphatase that modulates cellular nutrient sensing and the control of energy metabolism during Legionella infection.

PubMed: 28842705
DOI: 10.1038/s41598-017-10249-6

実験手法

X-RAY DIFFRACTION (1.7 Å)