4JGX

The Structure of Sterol Carrier Protein 2 from the Yeast Yarrowia Lipolytica

4JGX の概要

• エントリーDOI: 10.2210/pdb4jgx/pdb
• 分子名称: Fatty acid-binding protein, CITRIC ACID, PALMITIC ACID, ... (4 entities in total)
• 機能のキーワード: lipid binding protein, non specific lipid transfer, long chain fatty acids and coa esters
• 由来する生物種: Yarrowia lipolytica (Yeast)
• 細胞内の位置: Peroxisome (Potential): P80547
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29007.25

構造登録者

De Berti, F.P.,Capaldi, S.,Acierno, J.P.,Klinke, S.,Monaco, H.L.,Ermacora, M.R. (登録日: 2013-03-04, 公開日: 2013-12-18, 最終更新日: 2023-11-08)

主引用文献

De Berti, F.P.,Capaldi, S.,Ferreyra, R.,Burgardt, N.,Acierno, J.P.,Klinke, S.,Monaco, H.L.,Ermacora, M.R.
The crystal structure of sterol carrier protein 2 from Yarrowia lipolytica and the evolutionary conservation of a large, non-specific lipid-binding cavity.
J.Struct.Funct.Genom., 14:145-153, 2013

PubMed Abstract: Sterol carrier protein 2 (SCP2), a small intracellular domain present in all forms of life, binds with high affinity a broad spectrum of lipids. Due to its involvement in the metabolism of long-chain fatty acids and cholesterol uptake, it has been the focus of intense research in mammals and insects; much less characterized are SCP2 from other eukaryotic cells and microorganisms. We report here the X-ray structure of Yarrowia lipolytica SCP2 (YLSCP2) at 2.2 Å resolution in complex with palmitic acid. This is the first fungal SCP2 structure solved, and it consists of the canonical five-stranded β-sheet covered on the internal face by a layer of five α-helices. The overall fold is conserved among the SCP2 family, however, YLSCP2 is most similar to the SCP2 domain of human MFE-2, a bifunctional enzyme acting on peroxisomal β-oxidation. We have identified the common structural elements defining the shape and volume of the large binding cavity in all species characterized. Moreover, we found that the cavity of the SCP2 domains is distinctly formed by carbon atoms, containing neither organized water nor rigid polar interactions with the ligand. These features are in contrast with those of fatty acid binding proteins, whose internal cavities are more polar and contain bound water. The results will help to design experiments to unveil the SCP2 function in very different cellular contexts and metabolic conditions.

PubMed: 24241823
DOI: 10.1007/s10969-013-9166-6

実験手法

X-RAY DIFFRACTION (2.2 Å)