3SC6
2.65 Angstrom resolution crystal structure of dTDP-4-dehydrorhamnose reductase (rfbD) from Bacillus anthracis str. Ames in complex with NADP
Summary for 3SC6
| Entry DOI | 10.2210/pdb3sc6/pdb |
| Descriptor | dTDP-4-dehydrorhamnose reductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | dtdp-4-dehydrorhamnose reductase, rfbd, structural genomics, infectious diseases, bacillus anthracis str. ames, rhamnose biosynthetic pathway, center for structural genomics of infectious diseases, csgid, rossmann fold, catalyzes formation of dtdp-4-dehydro-6-deoxy-l-mannose, nadph and h+ from dtdp-6-deoxy-l-mannose and nadp+, oxidoreductase |
| Biological source | Bacillus anthracis (anthrax, anthrax bacterium) |
| Total number of polymer chains | 6 |
| Total formula weight | 202420.32 |
| Authors | Halavaty, A.S.,Kuhn, M.,Shuvalova, L.,Minasov, G.,Peterson, S.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2011-06-07, release date: 2011-06-22, Last modification date: 2023-09-13) |
| Primary citation | Law, A.,Stergioulis, A.,Halavaty, A.S.,Minasov, G.,Anderson, W.F.,Kuhn, M.L. Structure of the Bacillus anthracis dTDP-L-rhamnose-biosynthetic enzyme dTDP-4-dehydrorhamnose reductase (RfbD). Acta Crystallogr F Struct Biol Commun, 73:644-650, 2017 Cited by PubMed 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-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 Mg, the protein lacks the conserved residues that coordinate Mg. PubMed: 29199984DOI: 10.1107/S2053230X17015746 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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