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TitleGlutathionylation primes soluble glyceraldehyde-3-phosphate dehydrogenase for late collapse into insoluble aggregates.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 116, Page 26057-26065, Year 2019
Publish dateFeb 28, 2019 (structure data deposition date)
AuthorsZaffagnini, M. / Marchand, C.H. / Malferrari, M. / Murail, S. / Bonacchi, S. / Genovese, D. / Montalti, M. / Venturoli, G. / Falini, G. / Baaden, M. ...Zaffagnini, M. / Marchand, C.H. / Malferrari, M. / Murail, S. / Bonacchi, S. / Genovese, D. / Montalti, M. / Venturoli, G. / Falini, G. / Baaden, M. / Lemaire, S.D. / Fermani, S. / Trost, P.
External linksProc. Natl. Acad. Sci. USA / PubMed:31772010
MethodsX-ray diffraction
Resolution2.993 - 3 Å
Structure data

PDB-6qun:
Crystal structure of AtGapC1 with the catalytic Cys149 irreversibly oxidized by H2O2 treatment
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-6quq:
Crystal structure of glutathionylated glycolytic glyceraldehyde-3- phosphate dehydrogenase from Arabidopsis thaliana (AtGAPC1)
Method: X-RAY DIFFRACTION / Resolution: 2.993 Å

Chemicals

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-GSH:
GLUTATHIONE

Source
  • arabidopsis thaliana (thale cress)
KeywordsOXIDOREDUCTASE / Rossman fold / NAD binding / Glycolytic process / oxidative stress / Hydrogen peroxide / oxidoreductase activity / NAD / cytosolic / glutathione

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