1VPD

X-Ray Crystal Structure of Tartronate Semialdehyde Reductase [Salmonella Typhimurium LT2]

Replaces:  1TEA

Summary for 1VPD

• Entry DOI: 10.2210/pdb1vpd/pdb
• Descriptor: TARTRONATE SEMIALDEHYDE REDUCTASE, CHLORIDE ION, L(+)-TARTARIC ACID, ... (4 entities in total)
• Functional Keywords: structural genomics, mcsg, protein structure initiative, reductase, tartronate, psi, midwest center for structural genomics, oxidoreductase
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 1
• Total formula weight: 31922.87

Authors

Osipiuk, J.,Zhou, M.,Moy, S.,Collart, F.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2004-10-22, release date: 2004-10-26, Last modification date: 2024-10-30)

Primary citation

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, 10:249-253, 2009

PubMed 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.

PubMed: 19184529
DOI: 10.1007/s10969-009-9059-x

Experimental method

X-RAY DIFFRACTION (1.65 Å)