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| | <StructureSection load='5wvr' size='340' side='right'caption='[[5wvr]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='5wvr' size='340' side='right'caption='[[5wvr]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wvr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_sphaerica Candida sphaerica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WVR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5WVR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wvr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis_NRRL_Y-1140 Kluyveromyces lactis NRRL Y-1140]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WVR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</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]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KLLA0_C04147g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284590 Candida sphaerica])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</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'>[http://proteopedia.org/fgij/fg.htm?mol=5wvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wvr OCA], [http://pdbe.org/5wvr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wvr RCSB], [http://www.ebi.ac.uk/pdbsum/5wvr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wvr 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=5wvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wvr OCA], [https://pdbe.org/5wvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wvr RCSB], [https://www.ebi.ac.uk/pdbsum/5wvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wvr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6CUK7_KLULA Q6CUK7_KLULA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Candida sphaerica]] | + | [[Category: Kluyveromyces lactis NRRL Y-1140]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Im, Y J]] | + | [[Category: Im YJ]] |
| - | [[Category: Manik, M K]] | + | [[Category: Manik MK]] |
| - | [[Category: Tong, J S]] | + | [[Category: Tong JS]] |
| - | [[Category: Yang, H S]] | + | [[Category: Yang HS]] |
| - | [[Category: Cholesterol]]
| + | |
| - | [[Category: Lipid binding protein]]
| + | |
| - | [[Category: Lipid transfer]]
| + | |
| - | [[Category: Oxysterol binding]]
| + | |
| Structural highlights
Function
Q6CUK7_KLULA
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Manik MK, Yang H, Tong J, Im YJ. Structure of Yeast OSBP-Related Protein Osh1 Reveals Key Determinants for Lipid Transport and Protein Targeting at the Nucleus-Vacuole Junction. Structure. 2017 Apr 4;25(4):617-629.e3. doi: 10.1016/j.str.2017.02.010. Epub 2017, Mar 16. PMID:28319008 doi:http://dx.doi.org/10.1016/j.str.2017.02.010
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