5ijh
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the SPX domain of the human phosphate transporter XPR1 in complex with a sulfate ion== | |
| + | <StructureSection load='5ijh' size='340' side='right' caption='[[5ijh]], [[Resolution|resolution]] 2.43Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ijh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IJH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IJH FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ijh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ijh OCA], [http://pdbe.org/5ijh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ijh RCSB], [http://www.ebi.ac.uk/pdbsum/5ijh PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/XPR1_HUMAN XPR1_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/XPR1_HUMAN XPR1_HUMAN]] Plays a role in phosphate homeostasis. Mediates phosphate export from the cell (PubMed:25938945). May function in G-protein coupled signal transduction (By similarity).[UniProtKB:Q9Z0U0]<ref>PMID:25938945</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Phosphorus is a macronutrient taken up by cells as inorganic phosphate (Pi). How cells sense cellular Pilevels 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), whose concentrations change in response to Piavailability. Substitutions of critical binding surface residues impair InsP binding in vitro, inorganic polyphosphate synthesis in yeast and Pitransport inArabidopsis In plants, InsPs trigger the association of SPX proteins with transcription factors to regulate Pistarvation responses. We propose that InsPs communicate cytosolic Pilevels to SPX domains and enable them to interact with a multitude of proteins to regulate Piuptake, transport and storage in fungi, plants and animals. | ||
| - | + | Control of eukaryotic phosphate homeostasis by inositol polyphosphate sensor domains.,Wild R, Gerasimaite R, Jung JY, Truffault V, Pavlovic I, Schmidt A, Saiardi A, Jessen HJ, Poirier Y, Hothorn M, Mayer A Science. 2016 Apr 14. pii: aad9858. PMID:27080106<ref>PMID:27080106</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5ijh" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Hothorn, M]] | [[Category: Hothorn, M]] | ||
| + | [[Category: Wild, R]] | ||
| + | [[Category: Alpha-helical hairpin]] | ||
| + | [[Category: Helical bundle]] | ||
| + | [[Category: Inositol phosphate binding]] | ||
| + | [[Category: Inositol phosphate binding protein]] | ||
| + | [[Category: Protein-protein interaction]] | ||
| + | [[Category: Signaling protein]] | ||
Revision as of 12:08, 13 May 2016
Structure of the SPX domain of the human phosphate transporter XPR1 in complex with a sulfate ion
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