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Structure paper

TitleStructure of Yeast OSBP-Related Protein Osh1 Reveals Key Determinants for Lipid Transport and Protein Targeting at the Nucleus-Vacuole Junction
Journal, issue, pagesStructure, Vol. 25, Page 617-629.e3, Year 2017
Publish dateOct 14, 2016 (structure data deposition date)
AuthorsManik, M.K. / Yang, H. / Tong, J. / Im, Y.J.
External linksStructure / PubMed:28319008
MethodsX-ray diffraction
Resolution1.5 - 3.508 Å
Structure data

PDB-5h28:
Crystal structure of Osh1 ANK domain from Saccharomyces cerevisia
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-5h2a:
Crystal structure of Osh1 ANK domain from Kluyveromyces lactis
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-5h2c:
Crystal structure of Saccharomyces cerevisiae Osh1 ANK - Nvj1
Method: X-RAY DIFFRACTION / Resolution: 3.508 Å

PDB-5h2d:
Crystal structure of Osh1 ORD domain in complex with ergosterol
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-5wvr:
Crystal structure of Osh1 ORD domain in complex with cholesterol
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-ERG:
ERGOSTEROL

ChemComp-SO4:
SULFATE ION

ChemComp-CLR:
CHOLESTEROL

Source
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • kluyveromyces lactis (yeast)
KeywordsLIPID BINDING PROTEIN / oxysterol binding / lipid transfer / ANK Nvj1 / ergosterol / cholesterol

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