Structural highlights
Publication Abstract from PubMed
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.
High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA.,Schoebel S, Blankenfeldt W, Goody RS, Itzen A EMBO Rep. 2010 Aug;11(8):598-604. Epub 2010 Jul 9. PMID:20616805[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schoebel S, Blankenfeldt W, Goody RS, Itzen A. High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA. EMBO Rep. 2010 Aug;11(8):598-604. Epub 2010 Jul 9. PMID:20616805 doi:10.1038/embor.2010.97
