Toward a structural understanding of the dehydratase mechanism

Abstract

dTDP-D-glucose 4,6-dehydratase (RmlB) was first identified in the L-rhamnose biosynthetic pathway, where it catalyzes the conversion of dTDP-D-glucose into dTDP-4-keto-6-deoxy-D-glucose. The structures of RmlB from Salmonella enterica serovar Typhimurium in complex with substrate deoxythymidine 5′-diphospho-D-glucose (dTDP-D-glucose) and deoxythymidine 5′-diphosphate (dTDP), and RmlB from Streptococcus suis serotype 2 in complex with dTDP-D-glucose, dTDP, and deoxythymidine 5′-diphospho-D-pyrano-xylose (dTDP-xylose) have all been solved at resolutions between 1.8 Å and 2.4 Å. The structures show that the active sites are highly conserved. Importantly, the structures show that the active site..