5iiq

From Proteopedia

(Difference between revisions)

Current revision

Structure of the SPX-TTM domain fragment of the yeast inorganic polyphophate polymerase Vtc4 (form B).

Structural highlights

5iiq is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.03Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VTC4_YEAST Component of the vacuolar transporter chaperone (VTC) complex, which plays a role in vacuolar membrane fusion. Required for SEC18/NSF activity in SNARE priming, membrane binding of LMA1 and V(0) trans-complex formation.^[1] ^[2] ^[3]

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^[4]

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

References

↑ Ogawa N, DeRisi J, Brown PO. New components of a system for phosphate accumulation and polyphosphate metabolism in Saccharomyces cerevisiae revealed by genomic expression analysis. Mol Biol Cell. 2000 Dec;11(12):4309-21. PMID:11102525
↑ Muller O, Bayer MJ, Peters C, Andersen JS, Mann M, Mayer A. The Vtc proteins in vacuole fusion: coupling NSF activity to V(0) trans-complex formation. EMBO J. 2002 Feb 1;21(3):259-69. PMID:11823419 doi:http://dx.doi.org/10.1093/emboj/21.3.259
↑ Muller O, Neumann H, Bayer MJ, Mayer A. Role of the Vtc proteins in V-ATPase stability and membrane trafficking. J Cell Sci. 2003 Mar 15;116(Pt 6):1107-15. PMID:12584253
↑ 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 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

Categories: Large Structures | Saccharomyces cerevisiae | Hothorn M | Wild R

@@ Line 1: / Line 1: @@
 ==Structure of the SPX-TTM domain fragment of the yeast inorganic polyphophate polymerase Vtc4 (form B).==
-<StructureSection load='5iiq' size='340' side='right' caption='[[5iiq]], [[Resolution|resolution]] 3.03&Aring;' scene=''>
+<StructureSection load='5iiq' size='340' side='right'caption='[[5iiq]], [[Resolution|resolution]] 3.03&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5iiq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IIQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IIQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5iiq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IIQ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <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]] 3.03&#8491;</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=5iiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iiq OCA], [http://pdbe.org/5iiq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iiq RCSB], [http://www.ebi.ac.uk/pdbsum/5iiq PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=5iiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iiq OCA], [https://pdbe.org/5iiq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iiq RCSB], [https://www.ebi.ac.uk/pdbsum/5iiq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iiq ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/VTC4_YEAST VTC4_YEAST]] Component of the vacuolar transporter chaperone (VTC) complex, which plays a role in vacuolar membrane fusion. Required for SEC18/NSF activity in SNARE priming, membrane binding of LMA1 and V(0) trans-complex formation.<ref>PMID:11102525</ref> <ref>PMID:11823419</ref> <ref>PMID:12584253</ref>
+[https://www.uniprot.org/uniprot/VTC4_YEAST VTC4_YEAST] Component of the vacuolar transporter chaperone (VTC) complex, which plays a role in vacuolar membrane fusion. Required for SEC18/NSF activity in SNARE priming, membrane binding of LMA1 and V(0) trans-complex formation.<ref>PMID:11102525</ref> <ref>PMID:11823419</ref> <ref>PMID:12584253</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Hothorn, M]]
+[[Category: Large Structures]]
-[[Category: Wild, R]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Alpha-helical hairpin]]
+[[Category: Hothorn M]]
-[[Category: Chaperone]]
+[[Category: Wild R]]
-[[Category: Helical bundle]]
-[[Category: Inositol phosphate binding]]
-[[Category: Protein-protein interaction]]
-[[Category: Transferase]]

5iiq

From Proteopedia

Current revision

Structure of the SPX-TTM domain fragment of the yeast inorganic polyphophate polymerase Vtc4 (form B).

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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