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EMBO Rep. 2010 Aug;11(8):598-604. doi: 10.1038/embor.2010.97. Epub 2010 Jul 9.

High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA.

Author information

1
Department of Physical Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, North Rhine-Westphalia, Germany.

Abstract

The DrrA protein of Legionella pneumophila is involved in mistargeting of endoplasmic reticulum-derived vesicles to Legionella-containing vacuoles through recruitment of the small GTPase Rab1. To this effect, DrrA binds specifically to phosphatidylinositol 4-phosphate (PtdIns(4)P) lipids on the cytosolic surface of the phagosomal membrane shortly after infection. In this study, we present the atomic structure of the PtdIns(4)P-binding domain of a protein (DrrA) from a human pathogen. A detailed kinetic investigation of its interaction with PtdIns(4)P reveals that DrrA binds to this phospholipid with, as yet unprecedented, high affinity, suggesting that DrrA can sense a very low abundance of the lipid.

PMID:
20616805
PMCID:
PMC2920447
DOI:
10.1038/embor.2010.97
[Indexed for MEDLINE]
Free PMC Article

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