View source for 1kc1

[[Image:1kc1.jpg|left|200px]]

 {{Structure
|PDB= 1kc1 |SIZE=350|CAPTION= <scene name='initialview01'>1kc1</scene>, resolution 2.60&Aring;
|SITE= 
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=NDP:NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'>NDP</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/dTDP-4-dehydrorhamnose_reductase dTDP-4-dehydrorhamnose reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.133 1.1.1.133] 
|GENE= rfbA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=602 Salmonella typhimurium])
}}

'''Crystal structure of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (RmlD) in complex with NADPH'''


==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==
1KC1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KC1 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:[http://www.ncbi.nlm.nih.gov/pubmed/12057193 12057193]
[[Category: Salmonella typhimurium]]
[[Category: Single protein]]
[[Category: dTDP-4-dehydrorhamnose reductase]]
[[Category: Blankenfeldt, W.]]
[[Category: Giraud, M F.]]
[[Category: Graninger, M.]]
[[Category: Kerr, I D.]]
[[Category: Leonard, G A.]]
[[Category: McMiken, H J.]]
[[Category: Messner, P.]]
[[Category: Naismith, J H.]]
[[Category: Whitfield, C.]]
[[Category: MG]]
[[Category: NDP]]
[[Category: SO4]]
[[Category: rossman-fold]]
[[Category: sugar-nucleotide-binding domain]]

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