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

Journal Article · Mon Nov 06 00:00:00 EST 2017 · Acta Crystallographica. Section F, Structural Biology Communications

DOI:https://doi.org/10.1107/S2053230X17015746· OSTI ID:1498424

Law, Ashley; Stergioulis, Alexander; Halavaty, Andrei S.; Minasov, George ; Anderson, Wayne F.; Kuhn, Misty L.

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⁺.

• Research Organization: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
• Sponsoring Organization: NIAIDNIH
• OSTI ID: 1498424
• Journal Information: Acta Crystallographica. Section F, Structural Biology Communications, Vol. 73, Issue 12; ISSN 2053-230X
• Publisher: International Union of Crystallography
• Country of Publication: United States
• Language: ENGLISH