1YB4

Crystal Structure of the Tartronic Semialdehyde Reductase from Salmonella typhimurium LT2

Summary for 1YB4

• Entry DOI: 10.2210/pdb1yb4/pdb
• Descriptor: tartronic semialdehyde reductase (2 entities in total)
• Functional Keywords: structural genomics, tartronic semialdehyde reductase, oxidoreductase, salmonella typhimurium lt2, psi, protein structure initiative, the midwest center for structural genomics, mcsg
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 2
• Total formula weight: 63593.56

Authors

Kim, Y.,Wu, R.,Collart, F.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2004-12-20, release date: 2005-02-01, Last modification date: 2011-07-13)

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 (2.4 Å)