1VPD

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

「1TEA」から置き換えられました

1VPD の概要

• エントリーDOI: 10.2210/pdb1vpd/pdb
• 分子名称: TARTRONATE SEMIALDEHYDE REDUCTASE, CHLORIDE ION, L(+)-TARTARIC ACID, ... (4 entities in total)
• 機能のキーワード: structural genomics, mcsg, protein structure initiative, reductase, tartronate, psi, midwest center for structural genomics, oxidoreductase
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31922.87

構造登録者

Osipiuk, J.,Zhou, M.,Moy, S.,Collart, F.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2004-10-22, 公開日: 2004-10-26, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.65 Å)