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5h28

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Crystal structure of Osh1 ANK domain from Saccharomyces cerevisia

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 <StructureSection load='5h28' size='340' side='right'caption='[[5h28]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5h28]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H28 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5H28 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5h28]] is a 1 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=5H28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H28 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h2a|5h2a]], [[5h2c|5h2c]], [[5h2d|5h2d]]</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]] 1.5&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SWH1, OSH1, YAR042W, YAR044W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=5h28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h28 OCA], [https://pdbe.org/5h28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h28 RCSB], [https://www.ebi.ac.uk/pdbsum/5h28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h28 ProSAT]</span></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=5h28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h28 OCA], [http://pdbe.org/5h28 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h28 RCSB], [http://www.ebi.ac.uk/pdbsum/5h28 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h28 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/OSH1_YEAST OSH1_YEAST]] Lipid-binding protein involved in maintenance of intracellular sterol distribution and homeostasis. Binds to phosphoinositides. May be involved in formation of PMN vesicles by altering the membrane lipid composition.<ref>PMID:15173322</ref>
+[https://www.uniprot.org/uniprot/OSH1_YEAST OSH1_YEAST] Lipid-binding protein involved in maintenance of intracellular sterol distribution and homeostasis. Binds to phosphoinositides. May be involved in formation of PMN vesicles by altering the membrane lipid composition.<ref>PMID:15173322</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Yeast Osh1 belongs to the oxysterol-binding protein (OSBP) family of proteins and contains multiple targeting modules optimized for lipid transport at the nucleus-vacuole junction (NVJ). The key determinants for NVJ targeting and the role of Osh1 at NVJs have remained elusive because of unknown lipid specificities. In this study, we determined the structures of the ankyrin repeat domain (ANK), and OSBP-related domain (ORD) of Osh1, in complex with Nvj1 and ergosterol, respectively. The Osh1 ANK forms a unique bi-lobed structure that recognizes a cytosolic helical segment of Nvj1. We discovered that Osh1 ORD binds ergosterol and phosphatidylinositol 4-phosphate PI(4)P in a competitive manner, suggesting counter-transport function of the two lipids. Ergosterol is bound to the hydrophobic pocket in a head-down orientation, and the structure of the PI(4)P-binding site in Osh1 is well conserved. Our results suggest that Osh1 performs non-vesicular transport of ergosterol and PI(4)P at the NVJ.
-Structure of Yeast OSBP-Related Protein Osh1 Reveals Key Determinants for Lipid Transport and Protein Targeting at the Nucleus-Vacuole Junction.,Manik MK, Yang H, Tong J, Im YJ Structure. 2017 Apr 4;25(4):617-629.e3. doi: 10.1016/j.str.2017.02.010. Epub 2017, Mar 16. PMID:28319008<ref>PMID:28319008</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5h28" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 26: / Line 16: @@
 __TOC__
 </StructureSection>
-[[Category: Baker's yeast]]
 [[Category: Large Structures]]
-[[Category: Im, Y J]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Manik, M K]]
+[[Category: Im YJ]]
-[[Category: Tong, J S]]
+[[Category: Manik MK]]
-[[Category: Yang, H S]]
+[[Category: Tong JS]]
-[[Category: Ank nvj1]]
+[[Category: Yang HS]]
-[[Category: Lipid binding protein]]
-[[Category: Lipid transfer]]
-[[Category: Oxysterol binding]]

5h28

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Crystal structure of Osh1 ANK domain from Saccharomyces cerevisia

Structural highlights

Function

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