1kc3
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(New page: 200px<br /><applet load="1kc3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kc3, resolution 2.70Å" /> '''Crystal structure of...)
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Revision as of 16:55, 20 November 2007
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Crystal structure of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) in complex with NADPH and dTDP-L-rhamnose
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
1KC3 is a Single protein structure of sequence from Salmonella typhimurium with MG, NDP and TRH as ligands. 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
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