Structure of the Bacillus anthracis dTDP-L-rhamnose-biosynthetic enzyme dTDP-4-dehydrorhamnose reductase (RfbD).

ABSTRACT: Bacillus anthracis is the causative agent of the deadly disease Anthrax. Its use in bioterrorism and its ability to re-emerge have brought renewed interest in this organism. B. anthracis is a Gram-positive bacterium that adds L-rhamnose to its cell-wall polysaccharides using the activated donor dTDP-?-L-rhamnose. The enzymes involved in the biosynthesis of the activated donor are absent in humans, which make them ideal targets for therapeutic development to combat pathogens. Here, the 2.65?Å resolution crystal structure of the fourth enzyme in the dTDP-?-L-rhamnose-biosynthetic pathway from B. anthracis, dTDP-4-dehydro-?-L-rhamnose reductase (RfbD), is presented in complex with NADP⁺. This enzyme catalyzes the reduction of dTDP-4-dehydro-?-L-rhamnose to dTDP-?-L-rhamnose. Although the protein was co-crystallized in the presence of Mg²⁺, the protein lacks the conserved residues that coordinate Mg²⁺.

SUBMITTER: Law A 

PROVIDER: S-EPMC5713668 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature