1EM2
Star-related lipid transport domain of MLN64
1EM2 の概要
| エントリーDOI | 10.2210/pdb1em2/pdb |
| 分子名称 | MLN64 PROTEIN, D(-)-TARTARIC ACID (3 entities in total) |
| 機能のキーワード | beta barrel, lipid binding protein |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Late endosome membrane; Multi-pass membrane protein: Q14849 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 26263.23 |
| 構造登録者 | |
| 主引用文献 | Tsujishita, Y.,Hurley, J.H. Structure and lipid transport mechanism of a StAR-related domain. Nat.Struct.Biol., 7:408-414, 2000 Cited by PubMed Abstract: The steroidogenic acute regulatory protein (StAR) regulates acute steroidogenesis in the adrenal cortex and gonads by promoting the translocation of cholesterol to the mitochondrial inner membrane where the first step in steriod biosynthesis is catalyzed. StAR-related lipid transfer (START) domains occur in proteins involved in lipid transport and metabolism, signal transduction, and transcriptional regulation. The 2.2 A resolution crystal structure of the START domain of human MLN64 reported here reveals an alpha/beta fold built around a U-shaped incomplete beta-barrel. The interior of the protein encompasses a 26 x 12 x 11 A hydrophobic tunnel that is large enough to bind a single cholesterol molecule. The StAR and MLN64 START domains bind 1 mole of 14C cholesterol per mole of protein in vitro. Based on the START domain structure and cholesterol binding stoichiometry, it is proposed that StAR acts by shuttling cholesterol molecules one at a time through the intermembrane space of the mitochondrion. PubMed: 10802740DOI: 10.1038/75192 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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