6AOK

Crystal structure of Legionella pneumophila effector Ceg4 with N-terminal TEV protease cleavage sequence

6AOK の概要

• エントリーDOI: 10.2210/pdb6aok/pdb
• 関連するPDBエントリー: 6AOJ
• 分子名称: Ceg4, MAGNESIUM ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: effector, legionella pneumophila, infection, had-like phosphatase, alpha/beta protein, phosphotyrosine, hydrolase
• 由来する生物種: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25833.95

構造登録者

Stogios, P.J.,Cuff, M.E.,Nocek, B.,Evdokimova, E.,Egorova, O.,Yim, V.,Di Leo, R.,Savchenko, A. (登録日: 2017-08-16, 公開日: 2018-01-10, 最終更新日: 2024-10-16)

主引用文献

Quaile, A.T.,Stogios, P.J.,Egorova, O.,Evdokimova, E.,Valleau, D.,Nocek, B.,Kompella, P.S.,Peisajovich, S.,Yakunin, A.F.,Ensminger, A.W.,Savchenko, A.
TheLegionella pneumophilaeffector Ceg4 is a phosphotyrosine phosphatase that attenuates activation of eukaryotic MAPK pathways.
J. Biol. Chem., 293:3307-3320, 2018

PubMed Abstract: Host colonization by Gram-negative pathogens often involves delivery of bacterial proteins called "effectors" into the host cell. The pneumonia-causing pathogen delivers more than 330 effectors into the host cell via its type IVB Dot/Icm secretion system. The collective functions of these proteins are the establishment of a replicative niche from which can recruit cellular materials to grow while evading lysosomal fusion inhibiting its growth. Using a combination of structural, biochemical, and approaches, we show that one of these translocated effector proteins, Ceg4, is a phosphotyrosine phosphatase harboring a haloacid dehalogenase-hydrolase domain. Ceg4 could dephosphorylate a broad range of phosphotyrosine-containing peptides and attenuated activation of MAPK-controlled pathways in both yeast and human cells. Our findings indicate that 's infectious program includes manipulation of phosphorylation cascades in key host pathways. The structural and functional features of the Ceg4 effector unraveled here provide first insight into its function as a phosphotyrosine phosphatase, paving the way to further studies into pathogenicity.

PubMed: 29301934
DOI: 10.1074/jbc.M117.812727

実験手法

X-RAY DIFFRACTION (1.88 Å)