1KC1

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

1KC1 の概要

• エントリーDOI: 10.2210/pdb1kc1/pdb
• 関連するPDBエントリー: 1KBZ 1KC0 1KC3
• 分子名称: dTDP-glucose oxidoreductase, MAGNESIUM ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: rossman-fold, sugar-nucleotide-binding domain, oxidoreductase
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33455.73

構造登録者

Blankenfeldt, W.,Kerr, I.D.,Giraud, M.F.,McMiken, H.J.,Leonard, G.A.,Whitfield, C.,Messner, P.,Graninger, M.,Naismith, J.H. (登録日: 2001-11-07, 公開日: 2002-06-28, 最終更新日: 2024-02-07)

主引用文献

Blankenfeldt, W.,Kerr, I.D.,Giraud, M.F.,McMiken, H.J.,Leonard, G.,Whitfield, C.,Messner, P.,Graninger, M.,Naismith, J.H.
Variation on a theme of SDR. dTDP-6-deoxy-L- lyxo-4-hexulose reductase (RmlD) shows a new Mg2+-dependent dimerization mode.
Structure, 10:773-786, 2002

PubMed Abstract: 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.

PubMed: 12057193
DOI: 10.1016/S0969-2126(02)00770-0

実験手法

X-RAY DIFFRACTION (2.6 Å)