Structural Insights into Ubiquinone Biosynthesis in Membranes

Abstract

Catalysis in the Membrane Enzymes in the UbiA superfamily of integral membrane proteins synthesize lipid-soluble aromatics such as ubiquinones and chlorophylls that function in energy storage and energy transfer in mitochondrial and chloroplast membranes. Cheng and Li (p. 878 ) report structures of an archaeal UbiA protein in both apo and substrate-bound states. The structures show a large active site with a lateral portal that is likely to give access to the long-chain isoprenoid substrates. The findings suggest a mechanism for substrate recognition and catalysis and can explain disease-related mutants in eukaryotic homologs.