6DEW
Structure of human COQ9 protein with bound isoprene.
6DEW の概要
| エントリーDOI | 10.2210/pdb6dew/pdb |
| 分子名称 | Ubiquinone biosynthesis protein COQ9, mitochondrial, SULFATE ION, Geraniol, ... (7 entities in total) |
| 機能のキーワード | coq biosynthesis, isoprene binding, lipid binding protein |
| 由来する生物種 | Homo sapiens (Human) |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 147279.29 |
| 構造登録者 | Bingman, C.A.,Lohman, D.C.,Smith, R.W.,Pagliarini, D.J. (登録日: 2018-05-13, 公開日: 2019-02-06, 最終更新日: 2023-10-11) |
| 主引用文献 | Lohman, D.C.,Aydin, D.,Von Bank, H.C.,Smith, R.W.,Linke, V.,Weisenhorn, E.,McDevitt, M.T.,Hutchins, P.,Wilkerson, E.M.,Wancewicz, B.,Russell, J.,Stefely, M.S.,Beebe, E.T.,Jochem, A.,Coon, J.J.,Bingman, C.A.,Dal Peraro, M.,Pagliarini, D.J. An Isoprene Lipid-Binding Protein Promotes Eukaryotic Coenzyme Q Biosynthesis. Mol.Cell, 73:763-774.e10, 2019 Cited by PubMed Abstract: The biosynthesis of coenzyme Q presents a paradigm for how cells surmount hydrophobic barriers in lipid biology. In eukaryotes, CoQ precursors-among nature's most hydrophobic molecules-must somehow be presented to a series of enzymes peripherally associated with the mitochondrial inner membrane. Here, we reveal that this process relies on custom lipid-binding properties of COQ9. We show that COQ9 repurposes the bacterial TetR fold to bind aromatic isoprenes with high specificity, including CoQ intermediates that likely reside entirely within the bilayer. We reveal a process by which COQ9 associates with cardiolipin-rich membranes and warps the membrane surface to access this cargo. Finally, we identify a molecular interface between COQ9 and the hydroxylase COQ7, motivating a model whereby COQ9 presents intermediates directly to CoQ enzymes. Overall, our results provide a mechanism for how a lipid-binding protein might access, select, and deliver specific cargo from a membrane to promote biosynthesis. PubMed: 30661980DOI: 10.1016/j.molcel.2018.11.033 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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