1N2S: Crystal Structure Of Dtdp-6-deoxy-l-lyxo-4-hexulose Reductase (rmld) In Complex With Nadh

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.
PDB ID: 1N2SDownload
MMDB ID: 21046
PDB Deposition Date: 2002/10/24
Updated in MMDB: 2013/11
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 1N2S: dimeric; determined by author
Molecular Components in 1N2S
Label Count Molecule
Proteins (2 molecules)
Dtdp-glucose Oxidoreductase(Gene symbol: rfbD)
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

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