The shikimate pathway links metabolism of carbohydrates to biosynthesis of aromatic compounds. In a sequence of seven steps, phosphoenolpyruvate and erythrose 4-phosphate are converted to chorismate, a precursor of the aromatic amino acids and many secondary aromatic metabolites. The shikimate pathway is essential for most bacteria and plants but absent in humans, making it an attractive target for the development of novel antibiotics. The third step in the pathway consists of the dehydration of dehydroquinate to dehydroshikimate. This reaction can be achieved independently by two distinct enzyme families. The protein structure presented here is representative of the type I enzyme. The structure displays a typical TIM barrel fold with eight parallel beta strands and a C-terminal active site. In its unliganded form a three residues near the active site are disordered and have not been modeled.