4PH7
Structure of Osh6p in complex with phosphatidylinositol 4-phosphate
4PH7 の概要
| エントリーDOI | 10.2210/pdb4ph7/pdb |
| 関連するPDBエントリー | 3SPW |
| 分子名称 | Oxysterol-binding protein homolog 6, (2R)-1-{[(R)-hydroxy{[(1R,2R,3R,4R,5S,6R)-2,3,5,6-tetrahydroxy-4-(phosphonooxy)cyclohexyl]oxy}phosphoryl]oxy}-3-(octadecanoyloxy)propan-2-yl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate (3 entities in total) |
| 機能のキーワード | transport protein, osh proteins phosphatidylinositol phosphate lipid transport, lipid transport |
| 由来する生物種 | Saccharomyces cerevisiae (Baker's yeast) |
| 細胞内の位置 | Endoplasmic reticulum membrane : Q02201 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 211104.51 |
| 構造登録者 | Delfosse, V.,Moser von Filseck, J.,Antonny, B.,Bourguet, W.,Drin, G. (登録日: 2014-05-05, 公開日: 2015-07-29, 最終更新日: 2023-12-20) |
| 主引用文献 | Moser von Filseck, J.,Copic, A.,Delfosse, V.,Vanni, S.,Jackson, C.L.,Bourguet, W.,Drin, G. INTRACELLULAR TRANSPORT. Phosphatidylserine transport by ORP/Osh proteins is driven by phosphatidylinositol 4-phosphate. Science, 349:432-436, 2015 Cited by PubMed Abstract: In eukaryotic cells, phosphatidylserine (PS) is synthesized in the endoplasmic reticulum (ER) but is highly enriched in the plasma membrane (PM), where it contributes negative charge and to specific recruitment of signaling proteins. This distribution relies on transport mechanisms whose nature remains elusive. Here, we found that the PS transporter Osh6p extracted phosphatidylinositol 4-phosphate (PI4P) and exchanged PS for PI4P between two membranes. We solved the crystal structure of Osh6p:PI4P complex and demonstrated that the transport of PS by Osh6p depends on PI4P recognition in vivo. Finally, we showed that the PI4P-phosphatase Sac1p, by maintaining a PI4P gradient at the ER/PM interface, drove PS transport. Thus, PS transport by oxysterol-binding protein-related protein (ORP)/oxysterol-binding homology (Osh) proteins is fueled by PI4P metabolism through PS/PI4P exchange cycles. PubMed: 26206936DOI: 10.1126/science.aab1346 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.55 Å) |
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