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Article

Structural basis for substrate recognition by a unique <i>Legionella</i> phosphoinositide phosphatase

7 Aug 2012

Abstract excerpt

Legionella pneumophila is an opportunistic intracellular pathogen that causes sporadic and epidemic cases of Legionnaires' disease. Emerging data suggest that Legionella infection involves the subversion of host phosphoinositide (PI) metabolism. However, how this bacterium actively manipulates PI lipids to benefit its infection is still an enigma. Here, we report that the L. pneumophila virulence factor SidF is a...

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PMID: 22872863
DOI: 10.1073/pnas.1207903109

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Structural basis for substrate recognition by a unique <i>Legionella</i> phosphoinositide phosphatasePMID 22872863Read ↗

Identification and Structural Characterization of a Legionella Phosphoinositide Phosphatase*Semantic proximity Read ↗

Solution structure of the phosphatidylinositol 3-phosphate binding domain from the <i>Legionella</i> effector SetASemantic proximity Read ↗

Anchors for Effectors: Subversion of Phosphoinositide Lipids by LegionellaSemantic proximity Read ↗

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PIKfyve/Fab1 is required for efficient V-ATPase and hydrolase delivery to phagosomes, phagosomal killing, and restriction of <i>Legionella</i> infectionSemantic proximity Read ↗

Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila.Semantic proximity Read ↗

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NAD(H)-mediated tetramerization controls the activity of <i>Legionella pneumophila</i> phospholipase PlaBSemantic proximity Read ↗

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