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Crystal Structure of the Tartronic Semialdehyde Reductase from Salmonella typhimurium LT2Crystal Structure of the Tartronic Semialdehyde Reductase from Salmonella typhimurium LT2
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 PubMedTartronate 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
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OCA- 2-hydroxy-3-oxopropionate reductase
- Salmonella enterica subsp. enterica serovar typhimurium str. lt2
- Collart, F.
- Joachimiak, A.
- Kim, Y.
- MCSG, Midwest Center for Structural Genomics.
- Wu, R.
- Mcsg
- Oxidoreductase
- Protein structure initiative
- Psi
- Salmonella typhimurium lt2
- Structural genomic
- Tartronic semialdehyde reductase
- The midwest center for structural genomic