Dihydrodipicolinate synthase (DHDPS) catalyses the rate-limiting step in the biosynthesis of meso-diaminopimelate and lysine. Here, the cloning, expression, purification and crystallization of DHDPS from the intracellular pathogen Legionella pneumophila are described. Crystals grown in the presence of high-molecular-weight PEG precipitant and magnesium chloride were found to diffract beyond 1.65 A resolution. The crystal lattice belonged to the hexagonal space group P6(1)22, with unit-cell parameters a=b=89.31, c=290.18 A, and contained two molecules in the asymmetric unit. The crystal structure was determined by molecular replacement using a single chain of Pseudomonas aeruginosa DHDPS as the search model.
|1177 - 1181
|Number of pages
|Acta Crystallographica Section F: Structural Biology Communications
|Published - 2013