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| | ==Crystal structure of Saccharomyces cerevisiae Osh1 ANK - Nvj1== | | ==Crystal structure of Saccharomyces cerevisiae Osh1 ANK - Nvj1== |
| - | <StructureSection load='5h2c' size='340' side='right' caption='[[5h2c]], [[Resolution|resolution]] 3.51Å' scene=''> | + | <StructureSection load='5h2c' size='340' side='right'caption='[[5h2c]], [[Resolution|resolution]] 3.51Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5h2c]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H2C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H2C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5h2c]] is a 2 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=5H2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H2C FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h2d|5h2d]], [[5h28|5h28]], [[5h2a|5h2a]]</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]] 3.508Å</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=5h2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h2c OCA], [http://pdbe.org/5h2c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h2c RCSB], [http://www.ebi.ac.uk/pdbsum/5h2c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h2c 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=5h2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h2c OCA], [https://pdbe.org/5h2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h2c RCSB], [https://www.ebi.ac.uk/pdbsum/5h2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h2c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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> [[http://www.uniprot.org/uniprot/NVJ1_YEAST NVJ1_YEAST]] Involved in the formation of nucleus-vacuole (NV) junctions during piecemeal microautophagy of the nucleus (PMN). NV junctions are interorganelle interfaces mediated by NVJ1 in the nuclear envelope and VAC8 on the vacuole membrane. Together, NVJ1 and VAC8 form Velcro-like patches through which teardrop-like portions of the nucleus are pinched off into the vacuolar lumen and degraded by the PMN process. Acts also as an outer-nuclear membrane receptor for OSH1 and TSC13.<ref>PMID:10888680</ref> <ref>PMID:12529432</ref> <ref>PMID:15367582</ref> <ref>PMID:15958487</ref> <ref>PMID:16912077</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;">
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| - | == Publication Abstract from PubMed ==
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| - | 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.
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| - | 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>
| + | ==See Also== |
| - | | + | *[[Oxysterol-binding protein homolog|Oxysterol-binding protein homolog]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 5h2c" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Im, Y J]] | + | [[Category: Large Structures]] |
| - | [[Category: Manik, M K]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Tong, J S]] | + | [[Category: Im YJ]] |
| - | [[Category: Yang, H S]] | + | [[Category: Manik MK]] |
| - | [[Category: Lipid binding protein]] | + | [[Category: Tong JS]] |
| - | [[Category: Lipid transfer]] | + | [[Category: Yang HS]] |
| - | [[Category: Oxysterol binding]]
| + | |
