8CO4

Crystal structure of apo S-nitrosoglutathione reductase from Arabidopsis thalina

Summary for 8CO4

• Entry DOI: 10.2210/pdb8co4/pdb
• Descriptor: Alcohol dehydrogenase class-3, ZINC ION, 1,2-ETHANEDIOL, ... (7 entities in total)
• Functional Keywords: oxidoreductase, nitrosoglutathione reductase, alcohol dehydrogenase class iii, metalloprotein, zinc-binding enzyme, rossman fold
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 4
• Total formula weight: 165728.52

Authors

Fermani, S.,Fanti, S.,Carloni, G.,Rossi, J.,Falini, G.,Zaffagnini, M. (deposition date: 2023-02-27, release date: 2024-02-21, Last modification date: 2024-05-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)