Abstract
Octaprenyl pyrophosphate synthase (OPPs), which belongs to the E-type prenyltransferase family, catalyses the successive condensation of farnesyl pyrophosphate with five isopentenyl pyrophosphate molecules to form trans-C40-octaprenyl pyrophosphate (OPP). OPP is essential for the biosynthesis of bacterial ubiquinone or menaquinone side chains, which play an important role in the electron-transport system. Here, Escherichia coli OPPs was expressed, purified and crystallized. The crystals, which belonged to the orthorhombic space group P2₁2₁2, with unit-cell parameters a=117.0, b=128.4, c=46.4 Å, were obtained by the sitting-drop vapour-diffusion method and diffracted to 2.2 Å resolution. Initial phase determination by molecular replacement (MR) clearly indicated that the crystal contained one homodimer per asymmetric unit. Further model building and structural refinement are in progress.