Summary for 3F7J
| Entry DOI | 10.2210/pdb3f7j/pdb |
| Related | 3b3d 3b3f |
| Descriptor | YvgN protein, NITRATE ION, POTASSIUM ION, ... (4 entities in total) |
| Functional Keywords | aldo-keto reductase, oxidoreductase |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 2 |
| Total formula weight | 64048.20 |
| Authors | Zhou, Y.F.,Lei, J.,Liang, Y.H.,Su, X.-D. (deposition date: 2008-11-09, release date: 2008-11-25, Last modification date: 2023-12-27) |
| Primary citation | 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 Cited by 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: 19585557DOI: 10.1002/pro.178 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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