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. 3-phosphoshikimate 1- carboxyvinyltransferase is the sixth enzyme in the shikimate pathway and catalyzes the conversion of shikimate-3-phosphate and phosphoenolpyruvate to 5-enolpyruvyl-3-shikimate phosphate. The enzyme consists of six βαβαββ motifs, three in both N- and C-terminal domains. In this unliganded structure the two domains are splayed outwards (more so than in reported homolog structures) and a unique domain-domain interface is observed. Additionally, there are significant structural differences in the position of two crucial negatively charged C-terminal active site residues, which are sequestered within secondary structure and removed from the active site.