4XU5
Crystal structure of MvINS bound to a bromine-derived 14C Diacylglycerol (DAG) at 2.1A resolution
4XU5 の概要
エントリーDOI | 10.2210/pdb4xu5/pdb |
関連するPDBエントリー | 4XU4 4XU6 4XU7 4XU8 4XU9 |
分子名称 | Uncharacterized protein, (2S)-1-[(13-bromotridecanoyl)oxy]-3-hydroxypropan-2-yl tetradecanoate, DECANE, ... (5 entities in total) |
機能のキーワード | unknown function |
由来する生物種 | Mycobacterium vanbaalenii PYR-1 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 23134.51 |
構造登録者 | |
主引用文献 | Ren, R.,Zhou, X.,He, Y.,Ke, M.,Wu, J.,Liu, X.,Yan, C.,Wu, Y.,Gong, X.,Lei, X.,Yan, S.F.,Radhakrishnan, A.,Yan, N. PROTEIN STRUCTURE. Crystal structure of a mycobacterial Insig homolog provides insight into how these sensors monitor sterol levels Science, 349:187-191, 2015 Cited by PubMed Abstract: Insulin-induced gene 1 (Insig-1) and Insig-2 are endoplasmic reticulum membrane-embedded sterol sensors that regulate the cellular accumulation of sterols. Despite their physiological importance, the structural information on Insigs remains limited. Here we report the high-resolution structures of MvINS, an Insig homolog from Mycobacterium vanbaalenii. MvINS exists as a homotrimer. Each protomer comprises six transmembrane segments (TMs), with TM3 and TM4 contributing to homotrimerization. The six TMs enclose a V-shaped cavity that can accommodate a diacylglycerol molecule. A homology-based structural model of human Insig-2, together with biochemical characterizations, suggest that the central cavity of Insig-2 accommodates 25-hydroxycholesterol, whereas TM3 and TM4 engage in Scap binding. These analyses provide an important framework for further functional and mechanistic understanding of Insig proteins and the sterol regulatory element-binding protein pathway. PubMed: 26160948DOI: 10.1126/science.aab1091 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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