3D3F

Crystal Structure of Yvgn and cofactor NADPH from Bacillus subtilis

3D3F の概要

• エントリーDOI: 10.2210/pdb3d3f/pdb
• 分子名称: YvgN protein, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• 機能のキーワード: aldo-keto reductase, oxidoreductase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64640.41

構造登録者

Zhou, Y.F.,Lei, J.,Su, X.D. (登録日: 2008-05-10, 公開日: 2009-04-28, 最終更新日: 2023-11-01)

主引用文献

Lei, J.,Zhou, Y.F.,Li, L.F.,Su, X.-D.
Structural and biochemical analyses of YvgN and YtbE from Bacillus subtilis
Protein Sci., 18:1792-1800, 2009

PubMed Abstract: Bacillus subtilis is one of the most studied gram-positive bacteria. In this work, YvgN and YtbE from B. subtilis, assigned as AKR5G1 and AKR5G2 of aldo-keto reductase (AKR) superfamily. AKR catalyzes the NADPH-dependent reduction of aldehyde or aldose substrates to alcohols. YvgN and YtbE were studied by crystallographic and enzymatic analyses. The apo structures of these proteins were determined by molecular replacement, and the structure of holoenzyme YvgN with NADPH was also solved, revealing the conformational changes upon cofactor binding. Our biochemical data suggest both YvgN and YtbE have preferential specificity for derivatives of benzaldehyde, such as nitryl or halogen group substitution at the 2 or 4 positions. These proteins also showed broad catalytic activity on many standard substrates of AKR, such as glyoxal, dihydroxyacetone, and DL-glyceraldehyde, suggesting a possible role in bacterial detoxification.

PubMed: 19585557
DOI: 10.1002/pro.178

実験手法

X-RAY DIFFRACTION (2.4 Å)