Membrane reconstitution of human dihydroorotate dehydrogenase using lipid-detergent micelles
Human dihydroorotate dehydrogenase (DHODH) is an integral membrane protein found in mitochondria involved in pyrimidine biosynthesis. It oxidizes dihydroorotate with the simultaneous reduction of ubiquinone (Coenzyme Q10). DHODH is a well-validated target for anti-inflammatory and anti-proliferative drugs. Mutations in DHODH cause Miller syndrome, a rare genetic disorder. We aim to investigate the mechanisms by which DHODH interacts with the lipids found in the inner mitochondrial membrane (IMM) and with ubiquinone in a non-crystalline, physiologically relevant membrane-bound state. We will reconstitute full-length DHODH into supported lipid bilayers mimicking the IMM by means detergent-assisted adsorption of micelles using dodecyl-D-maltoside (DDM). The micelles will be characterized by small-angle neutron scattering (SANS) and the reconstituted enzyme will be analyzed by neutron reflectometry (NR). The resulting structures will expand the information available for truncated variants of DHODH.
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KNECHT Wolfgang; CORANI Alice; FRAGNETO Giovanna; MARTEL Anne; MICCIULLA Samantha; OROZCO RODRIGUEZ Juan Manuel; SCHNEIDER Harald and WACKLIN KNECHT Hanna. (2020). Membrane reconstitution of human dihydroorotate dehydrogenase using lipid-detergent micelles. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-02-879
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