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Publication Abstract from PubMed
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.
X-Ray crystal structure of GarR-tartronate semialdehyde reductase from Salmonella typhimurium.,Osipiuk J, Zhou M, Moy S, Collart F, Joachimiak A J Struct Funct Genomics. 2009 Jan 28. PMID:19184529[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Osipiuk J, Zhou M, Moy S, Collart F, Joachimiak A. X-Ray crystal structure of GarR-tartronate semialdehyde reductase from Salmonella typhimurium. J Struct Funct Genomics. 2009 Jan 28. PMID:19184529 doi:10.1007/s10969-009-9059-x
