Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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
