ArticleThe EMBO journal2013
Structure of the Legionella effector AnkX reveals the mechanism of phosphocholine transfer by the FIC domain.
Article in The EMBO journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 75 citations in OpenAlex.
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- Functions of Arabidopsis CTP:phosphocholine cytidylyltransferase 1 in phosphatidylcholine biosynthesis and root growth.Plant physiology · 2025Article
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- Genetic evidence for a regulated cysteine protease catalytic triad in LegA7, abioRxiv : the preprint server for biology · 2024Article
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- Legionella pneumophila-mediated host posttranslational modifications.Journal of molecular cell biology · 2023Review
- Legionella- and host-driven lipid flux at LCV-ER membrane contact sites promotes vacuole remodeling.EMBO reports · 2023Article
- AMPylation of small GTPases by Fic enzymes.FEBS letters · 2023Review
- Analysis of the Type 4 Effectome across the GenusInternational journal of molecular sciences · 2022Article
- Remnants of horizontal transfers of Wolbachia genes in a Wolbachia-free woodwasp.BMC ecology and evolution · 2022Article
- Diversity and function of arthropod endosymbiont toxins.Trends in microbiology · 2022Review
- Evolutionary Diversification of Host-TargetedMicroorganisms · 2021Article
- Manipulation of IRE1-Dependent MAPK Signaling by a Vibrio Agonist-Antagonist Effector Pair.mSystems · 2021Article
- Interesting Biochemistries in the Structure and Function of Bacterial Effectors.Frontiers in cellular and infection microbiology · 2021Review
- Bacterial virulence mediated by orthogonal post-translational modification.Nature chemical biology · 2020Review
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- Phosphoinositides and the Fate ofFrontiers in immunology · 2020Review
- Study ofInfection and immunity · 2019Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
The FIC motif and the eukaryotic-like ankyrin repeats are found in many bacterial type IV effectors, yet little is known about how these domains enable bacteria to modulate host cell functions. Bacterial FIC domains typically bind ATP and transfer adenosine monophosphate moiety onto target proteins. The ankyrin repeat-containing protein AnkX encoded by the intracellular pathogen Legionella pneumophila is unique in that its FIC domain binds to CDP-choline and transfers a phosphocholine residue onto proteins in the Rab1 GTPase family. By determining the structures of unbound AnkX and AnkX with bound CDP-choline, CMP/phosphocholine and CMP, we demonstrate that the orientation of substrate binding in relation to the catalytic FIC motif enables this protein to function as a phosphocholinating enzyme rather than a nucleotidyl transferase. Additionally, the structure reveals that the ankyrin repeats mediate scaffolding interactions that resemble those found in protein-protein interactions, but are unprecedented in intramolecular interactions. Together with phosphocholination experiments, our structures unify a general phosphoryl transferase mechanism common to all FIC enzymes that should be conserved from bacteria to human.
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