6CGK

Structure of the HAD domain of effector protein Lem4 (lpg1101) from Legionella pneumophila (inactive mutant)with phosphate bound in the active site

6CGK の概要

• エントリーDOI: 10.2210/pdb6cgk/pdb
• 関連するPDBエントリー: 6CDW 6CGJ
• 分子名称: effector protein Lem4 (lpg1101), PHOSPHATE ION, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: haloacid dehalogenase superfamily, tyrosine phosphatase, translocated bacterial effector, hydrolase
• 由来する生物種: Legionella pneumophila subsp. pneumophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24916.20

構造登録者

Beyrakhova, K.A.,Xu, C.,Cygler, M. (登録日: 2018-02-20, 公開日: 2018-07-18, 最終更新日: 2023-10-04)

主引用文献

Beyrakhova, K.,Li, L.,Xu, C.,Gagarinova, A.,Cygler, M.
Legionella pneumophilaeffector Lem4 is a membrane-associated protein tyrosine phosphatase.
J. Biol. Chem., 293:13044-13058, 2018

PubMed Abstract: is a Gram-negative pathogenic bacterium that causes severe pneumonia in humans. It establishes a replicative niche called -containing vacuole (LCV) that allows bacteria to survive and replicate inside pulmonary macrophages. To hijack host cell defense systems, injects over 300 effector proteins into the host cell cytosol. The Lem4 effector (lpg1101) consists of two domains: an N-terminal haloacid dehalogenase (HAD) domain with unknown function and a C-terminal phosphatidylinositol 4-phosphate-binding domain that anchors Lem4 to the membrane of early LCVs. Herein, we demonstrate that the HAD domain (Lem4-N) is structurally similar to mouse MDP-1 phosphatase and displays phosphotyrosine phosphatase activity. Substrate specificity of Lem4 was probed using a tyrosine phosphatase substrate set, which contained a selection of 360 phosphopeptides derived from human phosphorylation sites. This assay allowed us to identify a consensus pTyr-containing motif. Based on the localization of Lem4 to lysosomes and to some extent to plasma membrane when expressed in human cells, we hypothesize that this protein is involved in protein-protein interactions with an LCV or plasma membrane-associated tyrosine-phosphorylated host target.

PubMed: 29976756
DOI: 10.1074/jbc.RA118.003845

実験手法

X-RAY DIFFRACTION (1.668 Å)