1n2s
From Proteopedia
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CRYSTAL STRUCTURE OF DTDP-6-DEOXY-L-LYXO-4-HEXULOSE REDUCTASE (RMLD) IN COMPLEX WITH NADH
Overview
dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) catalyzes the final step, in the conversion of dTDP-D-glucose to dTDP-L-rhamnose in an NAD(P)H- and, Mg2+-dependent reaction. L-rhamnose biosynthesis is an antibacterial, target. The structure of RmlD from Salmonella enterica serovar Typhimurium, has been determined, and complexes with NADH, NADPH, and dTDP-L-rhamnose, are reported. RmlD differs from other short chain dehydrogenases in that, it has a novel dimer interface that contains Mg2+. Enzyme catalysis, involves hydride transfer from the nicotinamide ring of the cofactor to, the C4'-carbonyl group of the substrate. The substrate is activated, through protonation by a conserved tyrosine. NAD(P)H is bound in a, solvent-exposed cleft, allowing facile replacement. We suggest a novel, role for the conserved serine/threonine residue of the catalytic triad of, SDR enzymes.
About this Structure
1N2S is a Single protein structure of sequence from Salmonella enterica subsp. enterica serovar typhimurium with MG, NAD and TRS as ligands. This structure superseeds the now removed PDB entry 1KC0. Active as dTDP-4-dehydrorhamnose reductase, with EC number 1.1.1.133 Full crystallographic information is available from OCA.
Reference
Variation on a theme of SDR. dTDP-6-deoxy-L- lyxo-4-hexulose reductase (RmlD) shows a new Mg2+-dependent dimerization mode., Blankenfeldt W, Kerr ID, Giraud MF, McMiken HJ, Leonard G, Whitfield C, Messner P, Graninger M, Naismith JH, Structure. 2002 Jun;10(6):773-86. PMID:12057193
Page seeded by OCA on Tue Nov 20 21:54:04 2007
Categories: Salmonella enterica subsp. enterica serovar typhimurium | Single protein | DTDP-4-dehydrorhamnose reductase | Blankenfeldt, W. | Giraud, M.F. | Graninger, M. | Kerr, I.D. | Leonard, G.A. | Mcmiken, H.J. | Messner, P. | Naismith, J.H. | Whitfield, C. | MG | NAD | TRS | Rossman-fold | Sugar-nucleotide-binding domain
