6AWL
Crystal structure of human Coq9
Summary for 6AWL
| Entry DOI | 10.2210/pdb6awl/pdb |
| Descriptor | Ubiquinone biosynthesis protein COQ9, mitochondrial, DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE, 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total) |
| Functional Keywords | tetr family, coenzyme q biosynthesis, lipid binding, structural genomics, psi-2, protein structure initiative, mitochondrial protein partnership, mpp, biosynthetic protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 72001.09 |
| Authors | Bingman, C.A.,Lohman, D.C.,Smith, R.W.,Pagliarini, D.J.,Mitochondrial Protein Partnership (MPP) (deposition date: 2017-09-05, release date: 2019-02-06, Last modification date: 2023-10-04) |
| Primary citation | 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-, 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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