Structure of E.coli undecaprenyl pyrophosphate synthase

Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis.

Triton X-100, PEG8000, ethylele glycol, HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

single-wavelength anomalous diffraction (SAD)

undecaprenyl pyrophosphate synthase(E.C.2.5.1.31)/ 2-(2-{2-[2-(2-{2-[2-(2-{2-[4-(1,1,3,3-TETRAMETHYL-BUTYL)-PHENOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL

The enzyme is a dimer, including chains
A and B in the asymmetric unit.

Rossmann fold, hydrophobic tunnel, product chain length, flexible loop, TRANSFERASE