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• W2051946314 abstract "Significance A long-standing question in the field of microbial pathogenesis is how virulence factors are regulated within host cells and how their activity is specifically directed toward a particular host cell compartment. Legionella pneumophila resolves this dilemma by tightly coupling the phospholipase A1 activity of one of its effectors, vacuolar protein sorting inhibitor protein D (VipD), to this protein’s interaction with endosomal host GTPases. We now present the crystal structure of VipD in complex with host cell Rab5c, providing a detailed look into the ingenious molecular mechanisms underlying the allosteric activation of a virulence factor by a host protein and its spatiotemporal regulation. These results open the path for the development of novel therapeutics aimed at blocking the VipD activation process rather than the enzyme’s active site." @default.
• W2051946314 created "2016-06-24" @default.
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• W2051946314 date "2014-08-11" @default.
• W2051946314 modified "2023-10-16" @default.
• W2051946314 title "Structural basis for the recruitment and activation of the <i>Legionella</i> phospholipase VipD by the host GTPase Rab5" @default.
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• W2051946314 doi "https://doi.org/10.1073/pnas.1405391111" @default.
• W2051946314 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4151760" @default.
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