5H2A

Crystal structure of Osh1 ANK domain from Kluyveromyces lactis

5H2A の概要

• エントリーDOI: 10.2210/pdb5h2a/pdb
• 関連するPDBエントリー: 5H2B 5H2C 5H2D
• 分子名称: KLLA0C04147p (2 entities in total)
• 機能のキーワード: oxysterol binding, lipid transfer, ank nvj1, lipid binding protein
• 由来する生物種: Kluyveromyces lactis (Yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61384.10

構造登録者

Im, Y.J.,Manik, M.K.,Yang, H.S.,Tong, J.S. (登録日: 2016-10-14, 公開日: 2017-05-10, 最終更新日: 2024-03-20)

主引用文献

Manik, M.K.,Yang, H.,Tong, J.,Im, Y.J.
Structure of Yeast OSBP-Related Protein Osh1 Reveals Key Determinants for Lipid Transport and Protein Targeting at the Nucleus-Vacuole Junction
Structure, 25:617-629.e3, 2017

PubMed 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.

PubMed: 28319008
DOI: 10.1016/j.str.2017.02.010

実験手法

X-RAY DIFFRACTION (1.9 Å)