6CAY

Crystal structure of the first StART-like domain of Ysp2p/Lam2p in its apo and ergosterol-bound state.

6CAY の概要

• エントリーDOI: 10.2210/pdb6cay/pdb
• 分子名称: Sterol-binding protein, ERGOSTEROL (3 entities in total)
• 機能のキーワード: membrane contact sites, lipid transport protein, cholesterol, start domain, endoplasmic reticulum, lipid binding protein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 77435.48

構造登録者

Horenkamp, F.A.,Valverde, D.P.,Reinisch, K.M. (登録日: 2018-02-01, 公開日: 2018-02-28, 最終更新日: 2024-11-13)

主引用文献

Horenkamp, F.A.,Valverde, D.P.,Nunnari, J.,Reinisch, K.M.
Molecular basis for sterol transport by StART-like lipid transfer domains.
EMBO J., 37:-, 2018

PubMed Abstract: Lipid transport proteins at membrane contact sites, where two organelles are closely apposed, play key roles in trafficking lipids between cellular compartments while distinct membrane compositions for each organelle are maintained. Understanding the mechanisms underlying non-vesicular lipid trafficking requires characterization of the lipid transporters residing at contact sites. Here, we show that the mammalian proteins in the lipid transfer proteins anchored at a membrane contact site (LAM) family, called GRAMD1a-c, transfer sterols with similar efficiency as the yeast orthologues, which have known roles in sterol transport. Moreover, we have determined the structure of a lipid transfer domain of the yeast LAM protein Ysp2p, both in its apo-bound and sterol-bound forms, at 2.0 Å resolution. It folds into a truncated version of the steroidogenic acute regulatory protein-related lipid transfer (StART) domain, resembling a lidded cup in overall shape. Ergosterol binds within the cup, with its 3-hydroxy group interacting with protein indirectly via a water network at the cup bottom. This ligand binding mode likely is conserved for the other LAM proteins and for StART domains transferring sterols.

PubMed: 29467216
DOI: 10.15252/embj.201798002

実験手法

X-RAY DIFFRACTION (2 Å)