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Structure paper

TitleStructural and biochemical characterization of Arabidopsis alcohol dehydrogenases reveals distinct functional properties but similar redox sensitivity.
Journal, issue, pagesPlant J., Vol. 118, Page 1054-1070, Year 2024
Publish dateFeb 27, 2023 (structure data deposition date)
AuthorsMeloni, M. / Rossi, J. / Fanti, S. / Carloni, G. / Tedesco, D. / Treffon, P. / Piccinini, L. / Falini, G. / Trost, P. / Vierling, E. ...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.
External linksPlant J. / PubMed:38308388
MethodsX-ray diffraction
Resolution1.7 - 1.9 Å
Structure data

PDB-8co4:
Crystal structure of apo S-nitrosoglutathione reductase from Arabidopsis thalina
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-8con:
Crystal structure of alcohol dehydrogenase from Arabidopsis thaliana in complex with NADH
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE

ChemComp-SO4:
SULFATE ION

Source
  • arabidopsis thaliana (thale cress)
KeywordsOXIDOREDUCTASE / nitrosoglutathione reductase / alcohol dehydrogenase class III / metalloprotein / zinc-binding enzyme / Rossman fold / alcohol dehydrogenase / Zn-binding dehydrogenase

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