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TitleMolecular and structural basis for nitrosoglutathione-dependent redox regulation of triosephosphate isomerase from Chlamydomonas reinhardtii.
Journal, issue, pagesPlant Sci., Vol. 362, Page 112768-112768, Year 2025
Publish dateMar 21, 2025 (structure data deposition date)
AuthorsMeloni, M. / Mattioli, E.J. / Fanti, S. / Peppi, G.M.E. / Bin, T. / Gabellini, G. / Tedesco, D. / Henri, J. / Trost, P. / Lemaire, S.D. ...Meloni, M. / Mattioli, E.J. / Fanti, S. / Peppi, G.M.E. / Bin, T. / Gabellini, G. / Tedesco, D. / Henri, J. / Trost, P. / Lemaire, S.D. / Calvaresi, M. / Fermani, S. / Zaffagnini, M.
External linksPlant Sci. / PubMed:40946919
MethodsX-ray diffraction
Resolution1.2 - 3.55 Å
Structure data

PDB-9qm7:
Crystal structure of S-nitrosylated triose phosphate isomerase from Chlamydomonas reinhardtii
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

PDB-9r6m:
Crystal structure of C14S mutant of triosephosphate isomerase from Chamydomonas reinhardtii
Method: X-RAY DIFFRACTION / Resolution: 3.55 Å

Chemicals

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-EPE:
4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / pH buffer*YM

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • chlamydomonas reinhardtii (plant)
KeywordsISOMERASE / TIM-barrel fold / S-nitrosylation / chloroplast / MUTANT

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