Structure of the Bacillus anthracis dTDP-l-rhamnose-biosynthetic enzyme dTDP-4-dehydrorhamnose reductase (RfbD)
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- β -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- β -l-rhamnose-biosynthetic pathway from B. anthracis, dTDP-4-dehydro- β -l-rhamnose reductase (RfbD), is presented in complex with NADP+. This enzyme catalyzes the reduction of dTDP-4-dehydro- β -l-rhamnose to dTDP- β -l-rhamnose. Although the protein was co-crystallized in the presence of Mg2+, the protein lacks the conserved residues that coordinate Mg2+.
Source: Acta Crystallographica Section F - Category: Biochemistry Authors: Law, A. Stergioulis, A. Halavaty, A.S. Minasov, G. Anderson, W.F. Kuhn, M.L. Tags: RfbD dTDP-4-dehydrorhamnose reductase Bacillus anthracis Anthrax research communications Source Type: research
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