3sc6

Publication Abstract from PubMed

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-beta-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 A resolution crystal structure of the fourth enzyme in the dTDP-beta-L-rhamnose-biosynthetic pathway from B. anthracis, dTDP-4-dehydro-beta-L-rhamnose reductase (RfbD), is presented in complex with NADP(+). This enzyme catalyzes the reduction of dTDP-4-dehydro-beta-L-rhamnose to dTDP-beta-L-rhamnose. Although the protein was co-crystallized in the presence of Mg(2+), the protein lacks the conserved residues that coordinate Mg(2+).

Structure of the Bacillus anthracis dTDP-L-rhamnose-biosynthetic enzyme dTDP-4-dehydrorhamnose reductase (RfbD).,Law A, Stergioulis A, Halavaty AS, Minasov G, Anderson WF, Kuhn ML Acta Crystallogr F Struct Biol Commun. 2017 Dec 1;73(Pt 12):644-650. doi:, 10.1107/S2053230X17015746. Epub 2017 Nov 6. PMID:29199984^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.