3d3f
From Proteopedia
Crystal Structure of Yvgn and cofactor NADPH from Bacillus subtilis
Structural highlights
FunctionGR_BACSU Reduces glyoxal and methylglyoxal. Is not involved in the vitamin B6 biosynthesis. 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 PubMedBacillus 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. Structural and biochemical analyses of YvgN and YtbE from Bacillus subtilis.,Lei J, Zhou YF, Li LF, Su XD Protein Sci. 2009 Aug;18(8):1792-800. PMID:19585557[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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