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TitleTwo new T-state crystal structures of maize C 4 -phosphoenolpyruvate carboxylase reveal and suggest novel structural features of the allosteric regulation and carboxylation step.
Journal, issue, pagesInt. J. Biol. Macromol., Page 135134-135134, Year 2024
Publish dateAug 20, 2019 (structure data deposition date)
AuthorsCarrizosa-Carbajal, E.I. / Gonzalez-Segura, L. / Munoz-Clares, R.A.
External linksInt. J. Biol. Macromol. / PubMed:39208913
MethodsX-ray diffraction
Resolution2.8 - 2.909 Å
Structure data

PDB-6u2t:
Crystal structure of the T-state of maize C4-phosphoenolpyruvate carboxylase in complex with malate
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-6v3o:
Crystal structure of the T-state of maize C4-phosphoenolpyruvate carboxylase in complex with citrate
Method: X-RAY DIFFRACTION / Resolution: 2.909 Å

Chemicals

ChemComp-MLT:
D-MALATE

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-FLC:
CITRATE ANION

ChemComp-PG0:
2-(2-METHOXYETHOXY)ETHANOL / inhibitor, precipitant*YM

Source
  • zea mays (maize)
KeywordsLYASE / C4 metabolism / allosteric regulation / R and T states / PLANT PROTEIN

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