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 , and as ligands. This structure supersedes 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 Thu Feb 21 14:01:38 2008
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
