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

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.

• Authors: Stefan Schoebel, Wulf Blankenfeldt, Roger S Goody, Aymelt Itzen
• Journal: EMBO reports (EMBO Rep) Vol. 11 Issue 8 Pg. 598-604 (Aug 2010) ISSN: 1469-3178 [Electronic] England
• PMID: 20616805 (Publication Type: Journal Article)

Chemical References

• Bacterial Proteins
• Guanine Nucleotide Exchange Factors
• Phosphatidylinositol Phosphates
• SidM protein, Legionella pneumophila
• phosphatidylinositol 4-phosphate
• rab1 GTP-Binding Proteins

Topics

• Bacterial Proteins (chemistry, metabolism)
• Binding Sites
• Crystallography, X-Ray
• Guanine Nucleotide Exchange Factors (chemistry, metabolism)
• Humans
• Legionella pneumophila (chemistry, metabolism, pathogenicity)
• Models, Molecular
• Molecular Sequence Data
• Phagocytosis (physiology)
• Phosphatidylinositol Phosphates (chemistry, metabolism)
• Protein Binding
• Protein Conformation
• Protein Interaction Domains and Motifs
• rab1 GTP-Binding Proteins (metabolism)