3N6O
Crystal structure of the GEF and P4M domain of DrrA/SidM from Legionella pneumophila
Summary for 3N6O
| Entry DOI | 10.2210/pdb3n6o/pdb |
| Descriptor | guanine nucleotide exchange factor, SULFATE ION (3 entities in total) |
| Functional Keywords | phosphatidylinositol-4-phosphate, membrane, gef, rab, lcv, p4m, rabgef, signaling protein |
| Biological source | Legionella pneumophila |
| Total number of polymer chains | 2 |
| Total formula weight | 71018.42 |
| Authors | Schoebel, S.,Blankenfeldt, W.,Goody, R.S.,Itzen, A. (deposition date: 2010-05-26, release date: 2010-07-28, Last modification date: 2024-02-21) |
| Primary citation | Schoebel, S.,Blankenfeldt, W.,Goody, R.S.,Itzen, A. High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA. Embo Rep., 11:598-604, 2010 Cited by PubMed 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. PubMed: 20616805DOI: 10.1038/embor.2010.97 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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