7W9Z

Crystal structure of Bacillus subtilis YugJ in complex with NADP and nitrate

7W9Z の概要

• エントリーDOI: 10.2210/pdb7w9z/pdb
• 分子名称: Iron-containing alcohol dehydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, NITRATE ION, ... (4 entities in total)
• 機能のキーワード: aldehyde reductase, oxidoreductase
• 由来する生物種: Bacillus subtilis subsp. spizizenii ATCC 6633
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 88353.17

構造登録者

Cho, H.Y.,Nam, M.S.,Hong, H.J.,Song, W.S.,Yoon, S.I. (登録日: 2021-12-11, 公開日: 2022-12-07, 最終更新日: 2023-11-29)

主引用文献

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

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: 35163804
DOI: 10.3390/ijms23031882

実験手法

X-RAY DIFFRACTION (1.65 Å)