8CON

Crystal structure of alcohol dehydrogenase from Arabidopsis thaliana in complex with NADH

8CON の概要

• エントリーDOI: 10.2210/pdb8con/pdb
• 関連するPDBエントリー: 8CO4
• 分子名称: Alcohol dehydrogenase class-P, ZINC ION, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, ... (8 entities in total)
• 機能のキーワード: oxidoreductase, alcohol dehydrogenase, zn-binding dehydrogenase, metalloprotein, rossman fold
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43849.16

構造登録者

Fermani, S.,Fanti, S.,Carloni, G.,Falini, G.,Meloni, M.,Zaffagnini, M. (登録日: 2023-02-28, 公開日: 2024-02-21, 最終更新日: 2025-10-01)

主引用文献

Meloni, M.,Rossi, J.,Fanti, S.,Carloni, G.,Tedesco, D.,Treffon, P.,Piccinini, L.,Falini, G.,Trost, P.,Vierling, E.,Licausi, F.,Giuntoli, B.,Musiani, F.,Fermani, S.,Zaffagnini, M.
Structural and biochemical characterization of Arabidopsis alcohol dehydrogenases reveals distinct functional properties but similar redox sensitivity.
Plant J., 118:1054-1070, 2024

PubMed Abstract: Alcohol dehydrogenases (ADHs) are a group of zinc-binding enzymes belonging to the medium-length dehydrogenase/reductase (MDR) protein superfamily. In plants, these enzymes fulfill important functions involving the reduction of toxic aldehydes to the corresponding alcohols (as well as catalyzing the reverse reaction, i.e., alcohol oxidation; ADH1) and the reduction of nitrosoglutathione (GSNO; ADH2/GSNOR). We investigated and compared the structural and biochemical properties of ADH1 and GSNOR from Arabidopsis thaliana. We expressed and purified ADH1 and GSNOR and determined two new structures, NADH-ADH1 and apo-GSNOR, thus completing the structural landscape of Arabidopsis ADHs in both apo- and holo-forms. A structural comparison of these Arabidopsis ADHs revealed a high sequence conservation (59% identity) and a similar fold. In contrast, a striking dissimilarity was observed in the catalytic cavity supporting substrate specificity and accommodation. Consistently, ADH1 and GSNOR showed strict specificity for their substrates (ethanol and GSNO, respectively), although both enzymes had the ability to oxidize long-chain alcohols, with ADH1 performing better than GSNOR. Both enzymes contain a high number of cysteines (12 and 15 out of 379 residues for ADH1 and GSNOR, respectively) and showed a significant and similar responsivity to thiol-oxidizing agents, indicating that redox modifications may constitute a mechanism for controlling enzyme activity under both optimal growth and stress conditions.

PubMed: 38308388
DOI: 10.1111/tpj.16651

実験手法

X-RAY DIFFRACTION (1.7 Å)