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TitleKinetic and structural studies of Trypanosoma and Leishmania phosphofructokinases show evolutionary divergence and identify AMP as a switch regulating glycolysis versus gluconeogenesis.
Journal, issue, pagesFebs J., Vol. 287, Page 2847-2861, Year 2020
Publish dateSep 27, 2019 (structure data deposition date)
AuthorsFernandes, P.M. / Kinkead, J. / McNae, I.W. / Vasquez-Valdivieso, M. / Wear, M.A. / Michels, P.A.M. / Walkinshaw, M.D.
External linksFebs J. / PubMed:31838765
MethodsX-ray diffraction
Resolution2.75 Å
Structure data

PDB-6sy7:
Structure of Trypanosome Brucei Phosphofructokinase in complex with AMP.
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

Chemicals

ChemComp-BNZ:
BENZENE

ChemComp-GOL:
GLYCEROL

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-HOH:
WATER

Source
  • trypanosoma brucei brucei (eukaryote)
KeywordsTRANSFERASE / Glycolysis / AMP / Allostery

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