5h2d | pdb_00005h2d

Crystal structure of Osh1 ORD domain in complex with ergosterol

spinqualitylabelsall models 5h2d, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5h2d is a 1 chain structure with sequence from Candida sphaerica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ERG, SO4 Related: 5h28, 5h2a, 5h2c Gene: KLLA0_C04147g (Candida sphaerica) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Oxysterol-binding protein homolog

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