PDBsum entry 5h28

Lipid binding protein

PDB id: 5h28

Contents

Protein chain

263 a.a.

Waters ×315

PDB id:

5h28

Name:

Lipid binding protein

Title:

Crystal structure of osh1 ank domain from saccharomyces cerevisia

Structure:

Oxysterol-binding protein homolog 1. Chain: a. Fragment: unp residues 12-274. Engineered: yes

Source:

Saccharomyces cerevisiae (strain atcc 204508 / s288c). Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: swh1, osh1, yar042w, yar044w. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.50Å R-factor: 0.184 R-free: 0.214

Authors:

Y.J.Im,M.K.Manik,H.S.Yang,J.S.Tong

Key ref:

M.K.Manik et al. (2017). Structure of Yeast OSBP-Related Protein Osh1 Reveals Key Determinants for Lipid Transport and Protein Targeting at the Nucleus-Vacuole Junction. Structure, 25, 617. PubMed id: 28319008 DOI: 10.1016/j.str.2017.02.010

Date:

14-Oct-16 Release date: 17-May-17

Protein chain

P35845  (OSH1_YEAST) -  Oxysterol-binding protein homolog 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 1188 a.a.

Struc: 263 a.a.

DOI no: 10.1016/j.str.2017.02.010

Structure 25:617 (2017)

PubMed id: 28319008

Structure of Yeast OSBP-Related Protein Osh1 Reveals Key Determinants for Lipid Transport and Protein Targeting at the Nucleus-Vacuole Junction.

M.K.Manik, H.Yang, J.Tong, Y.J.Im.

ABSTRACT

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.