5ijh

From Proteopedia

(Difference between revisions)

Current revision

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

Structural highlights

5ijh is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.43Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

S53A1_HUMAN Bilateral striopallidodentate calcinosis. The disease is caused by variants affecting the gene represented in this entry.

Function

S53A1_HUMAN Inorganic ion transporter that mediates phosphate ion export across plasma membrane. Plays a major role in phosphate homeostasis, preventing intracellular phosphate accumulation and possible calcium phosphate precipitation, ultimately preserving calcium signaling. The molecular mechanism of phosphate transport, whether electrogenic, electroneutral or coupled to other ions, remains to be elucidated (By similarity) (PubMed:23791524, PubMed:25938945, PubMed:31043717). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7), important intracellular signaling molecules involved in regulation of phosphate flux (PubMed:27080106).[UniProtKB:Q9Z0U0]^[1] ^[2] ^[3] ^[4]

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^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Giovannini D, Touhami J, Charnet P, Sitbon M, Battini JL. Inorganic phosphate export by the retrovirus receptor XPR1 in metazoans. Cell Rep. 2013 Jun 27;3(6):1866-73. PMID:23791524 doi:10.1016/j.celrep.2013.05.035
↑ Legati A, Giovannini D, Nicolas G, Lopez-Sanchez U, Quintans B, Oliveira JR, Sears RL, Ramos EM, Spiteri E, Sobrido MJ, Carracedo A, Castro-Fernandez C, Cubizolle S, Fogel BL, Goizet C, Jen JC, Kirdlarp S, Lang AE, Miedzybrodzka Z, Mitarnun W, Paucar M, Paulson H, Pariente J, Richard AC, Salins NS, Simpson SA, Striano P, Svenningsson P, Tison F, Unni VK, Vanakker O, Wessels MW, Wetchaphanphesat S, Yang M, Boller F, Campion D, Hannequin D, Sitbon M, Geschwind DH, Battini JL, Coppola G. Mutations in XPR1 cause primary familial brain calcification associated with altered phosphate export. Nat Genet. 2015 Jun;47(6):579-81. doi: 10.1038/ng.3289. Epub 2015 May 4. PMID:25938945 doi:http://dx.doi.org/10.1038/ng.3289
↑ Wild R, Gerasimaite R, Jung JY, Truffault V, Pavlovic I, Schmidt A, Saiardi A, Jessen HJ, Poirier Y, Hothorn M, Mayer A. Control of eukaryotic phosphate homeostasis by inositol polyphosphate sensor domains. Science. 2016 Apr 14. pii: aad9858. PMID:27080106 doi:http://dx.doi.org/10.1126/science.aad9858
↑ López-Sánchez U, Nicolas G, Richard AC, Maltête D, Charif M, Ayrignac X, Goizet C, Touhami J, Labesse G, Battini JL, Sitbon M. Characterization of XPR1/SLC53A1 variants located outside of the SPX domain in patients with primary familial brain calcification. Sci Rep. 2019 May 1;9(1):6776. PMID:31043717 doi:10.1038/s41598-019-43255-x
↑ Wild R, Gerasimaite R, Jung JY, Truffault V, Pavlovic I, Schmidt A, Saiardi A, Jessen HJ, Poirier Y, Hothorn M, Mayer A. Control of eukaryotic phosphate homeostasis by inositol polyphosphate sensor domains. Science. 2016 Apr 14. pii: aad9858. PMID:27080106 doi:http://dx.doi.org/10.1126/science.aad9858

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ijh"

Categories: Homo sapiens | Large Structures | Hothorn M | Wild R

@@ Line 3: / Line 3: @@
 <StructureSection load='5ijh' size='340' side='right'caption='[[5ijh]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ijh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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://proteopedia.org/fgij/fg.htm?mol=5IJH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ijh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5IJH FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.43&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XPR1, SYG1, XR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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://proteopedia.org/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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ijh ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ijh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ijh OCA], [https://pdbe.org/5ijh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ijh RCSB], [https://www.ebi.ac.uk/pdbsum/5ijh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ijh ProSAT]</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.
+[https://www.uniprot.org/uniprot/S53A1_HUMAN S53A1_HUMAN] Bilateral striopallidodentate calcinosis. The disease is caused by variants 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>
+[https://www.uniprot.org/uniprot/S53A1_HUMAN S53A1_HUMAN] Inorganic ion transporter that mediates phosphate ion export across plasma membrane. Plays a major role in phosphate homeostasis, preventing intracellular phosphate accumulation and possible calcium phosphate precipitation, ultimately preserving calcium signaling. The molecular mechanism of phosphate transport, whether electrogenic, electroneutral or coupled to other ions, remains to be elucidated (By similarity) (PubMed:23791524, PubMed:25938945, PubMed:31043717). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7), important intracellular signaling molecules involved in regulation of phosphate flux (PubMed:27080106).[UniProtKB:Q9Z0U0]<ref>PMID:23791524</ref> <ref>PMID:25938945</ref> <ref>PMID:27080106</ref> <ref>PMID:31043717</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 25: / Line 25: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Hothorn, M]]
+[[Category: Hothorn M]]
-[[Category: Wild, R]]
+[[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]]

5ijh

From Proteopedia

Current revision

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

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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