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5IJH

Structure of the SPX domain of the human phosphate transporter XPR1 in complex with a sulfate ion

Summary for 5IJH
Entry DOI10.2210/pdb5ijh/pdb
DescriptorXenotropic and polytropic retrovirus receptor 1, SULFATE ION (3 entities in total)
Functional Keywordshelical bundle, alpha-helical hairpin, inositol phosphate binding, protein-protein interaction, signaling protein, inositol phosphate binding protein
Biological sourceHomo sapiens (Human)
Cellular locationCell membrane ; Multi-pass membrane protein : Q9UBH6
Total number of polymer chains2
Total formula weight50909.54
Authors
Wild, R.,Hothorn, M. (deposition date: 2016-03-02, release date: 2016-04-27, Last modification date: 2024-10-16)
Primary citationWild, R.,Gerasimaite, R.,Jung, J.Y.,Truffault, V.,Pavlovic, I.,Schmidt, A.,Saiardi, A.,Jessen, H.J.,Poirier, Y.,Hothorn, M.,Mayer, A.
Control of eukaryotic phosphate homeostasis by inositol polyphosphate sensor domains.
Science, 352:986-990, 2016
Cited by
PubMed Abstract: Phosphorus is a macronutrient taken up by cells as inorganic phosphate (P(i)). How cells sense cellular P(i) levels is poorly characterized. Here, we report that SPX domains--which are found in eukaryotic phosphate transporters, signaling proteins, and inorganic polyphosphate polymerases--provide a basic binding surface for inositol polyphosphate signaling molecules (InsPs), the concentrations of which change in response to P(i) availability. Substitutions of critical binding surface residues impair InsP binding in vitro, inorganic polyphosphate synthesis in yeast, and P(i) transport in Arabidopsis In plants, InsPs trigger the association of SPX proteins with transcription factors to regulate P(i) starvation responses. We propose that InsPs communicate cytosolic P(i) levels to SPX domains and enable them to interact with a multitude of proteins to regulate P(i) uptake, transport, and storage in fungi, plants, and animals.
PubMed: 27080106
DOI: 10.1126/science.aad9858
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.43 Å)
Structure validation

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