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X-ray crystal structure of GarR-tartronate semialdehyde reductase from Salmonella typhimurium.

ABSTRACT: Tartronate semialdehyde reductases (TSRs), also known as 2-hydroxy-3-oxopropionate reductases, catalyze the reduction of tartronate semialdehyde using NAD as cofactor in the final stage of D-glycerate biosynthesis. These enzymes belong to family of structurally and mechanically related beta-hydroxyacid dehydrogenases which differ in substrate specificity and catalyze reactions in specific metabolic pathways. Here, we present the crystal structure of GarR a TSR from Salmonella typhimurium determined by the single-wavelength anomalous diffraction method and refined to 1.65 A resolution. The active site of the enzyme contains L-tartrate which most likely mimics a position of a glycerate which is a product of the enzyme reaction. The analysis of the TSR structure shows also a putative NADPH binding site in the enzyme.

SUBMITTER: Osipiuk J

PROVIDER: S-EPMC2791999 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature

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X-ray crystal structure of GarR-tartronate semialdehyde reductase from Salmonella typhimurium.

Osipiuk J J Zhou M M Moy S S Collart F F Joachimiak A A

Journal of structural and functional genomics 20090128 3

Tartronate semialdehyde reductases (TSRs), also known as 2-hydroxy-3-oxopropionate reductases, catalyze the reduction of tartronate semialdehyde using NAD as cofactor in the final stage of D-glycerate biosynthesis. These enzymes belong to family of structurally and mechanically related beta-hydroxyacid dehydrogenases which differ in substrate specificity and catalyze reactions in specific metabolic pathways. Here, we present the crystal structure of GarR a TSR from Salmonella typhimurium determi ...[more]

PMID: 19184529

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