View source for 4ph7


==Structure of Osh6p in complex with phosphatidylinositol 4-phosphate==
<StructureSection load='4ph7' size='340' side='right'caption='[[4ph7]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ph7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PH7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PH7 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2Y5:(2R)-1-{[(R)-HYDROXY{[(1R,2R,3R,4R,5S,6R)-2,3,5,6-TETRAHYDROXY-4-(PHOSPHONOOXY)CYCLOHEXYL]OXY}PHOSPHORYL]OXY}-3-(OCTADECANOYLOXY)PROPAN-2-YL+(5Z,8Z,11Z,14Z)-ICOSA-5,8,11,14-TETRAENOATE'>2Y5</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=4ph7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ph7 OCA], [https://pdbe.org/4ph7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ph7 RCSB], [https://www.ebi.ac.uk/pdbsum/4ph7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ph7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OSH6_YEAST OSH6_YEAST] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In eukaryotic cells, phosphatidylserine (PS) is synthesized in the endoplasmic reticulum (ER) but is highly enriched in the plasma membrane (PM), where it contributes negative charge and to specific recruitment of signaling proteins. This distribution relies on transport mechanisms whose nature remains elusive. Here, we found that the PS transporter Osh6p extracted phosphatidylinositol 4-phosphate (PI4P) and exchanged PS for PI4P between two membranes. We solved the crystal structure of Osh6p:PI4P complex and demonstrated that the transport of PS by Osh6p depends on PI4P recognition in vivo. Finally, we showed that the PI4P-phosphatase Sac1p, by maintaining a PI4P gradient at the ER/PM interface, drove PS transport. Thus, PS transport by oxysterol-binding protein-related protein (ORP)/oxysterol-binding homology (Osh) proteins is fueled by PI4P metabolism through PS/PI4P exchange cycles.

INTRACELLULAR TRANSPORT. Phosphatidylserine transport by ORP/Osh proteins is driven by phosphatidylinositol 4-phosphate.,Moser von Filseck J, Copic A, Delfosse V, Vanni S, Jackson CL, Bourguet W, Drin G Science. 2015 Jul 24;349(6246):432-6. doi: 10.1126/science.aab1346. Epub 2015 Jul, 23. PMID:26206936<ref>PMID:26206936</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ph7" style="background-color:#fffaf0;"></div>

==See Also==
*[[Oxysterol-binding protein homolog|Oxysterol-binding protein homolog]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Antonny B]]
[[Category: Bourguet W]]
[[Category: Delfosse V]]
[[Category: Drin G]]
[[Category: Moser von Filseck J]]