7W9Y
Crystal structure of Bacillus subtilis YugJ in complex with NADP and nickel
Summary for 7W9Y
| Entry DOI | 10.2210/pdb7w9y/pdb |
| Descriptor | Iron-containing alcohol dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, NICKEL (II) ION, ... (4 entities in total) |
| Functional Keywords | aldehyde reductase, oxidoreductase |
| Biological source | Bacillus subtilis subsp. spizizenii ATCC 6633 |
| Total number of polymer chains | 4 |
| Total formula weight | 176445.08 |
| Authors | Cho, H.Y.,Nam, M.S.,Hong, H.J.,Song, W.S.,Yoon, S.I. (deposition date: 2021-12-11, release date: 2022-12-07, Last modification date: 2023-11-29) |
| Primary citation | Cho, H.Y.,Nam, M.S.,Hong, H.J.,Song, W.S.,Yoon, S.I. Structural and Biochemical Analysis of the Furan Aldehyde Reductase YugJ from Bacillus subtilis. Int J Mol Sci, 23:-, 2022 Cited by PubMed Abstract: NAD(H)/NADP(H)-dependent aldehyde/alcohol oxidoreductase (AAOR) participates in a wide range of physiologically important cellular processes by reducing aldehydes or oxidizing alcohols. Among AAOR substrates, furan aldehyde is highly toxic to microorganisms. To counteract the toxic effect of furan aldehyde, some bacteria have evolved AAOR that converts furan aldehyde into a less toxic alcohol. Based on biochemical and structural analyses, we identified YugJ as an atypical AAOR that reduces furan aldehyde. YugJ displayed high substrate specificity toward 5-hydroxymethylfurfural (HMF), a furan aldehyde, in an NADPH- and Ni-dependent manner. YugJ folds into a two-domain structure consisting of a Rossmann-like domain and an α-helical domain. YugJ interacts with NADP and Ni using the interdomain cleft of YugJ. A comparative analysis of three YugJ structures indicated that NADP(H) binding plays a key role in modulating the interdomain dynamics of YugJ. Noticeably, a nitrate ion was found in proximity to the nicotinamide ring of NADP in the YugJ structure, and the HMF-reducing activity of YugJ was inhibited by nitrate, providing insights into the substrate-binding mode of YugJ. These findings contribute to the characterization of the YugJ-mediated furan aldehyde reduction mechanism and to the rational design of improved furan aldehyde reductases for the biofuel industry. PubMed: 35163804DOI: 10.3390/ijms23031882 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.93 Å) |
Structure validation
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