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Structure paper

Title`In crystallo' substrate binding triggers major domain movements and reveals magnesium as a co-activator of Trypanosoma brucei pyruvate kinase.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 69, Page 1768-1779, Year 2013
Publish dateNov 14, 2012 (structure data deposition date)
AuthorsZhong, W. / Morgan, H.P. / McNae, I.W. / Michels, P.A. / Fothergill-Gilmore, L.A. / Walkinshaw, M.D.
External linksActa Crystallogr. ,Sect. D / PubMed:23999300
MethodsX-ray diffraction
Resolution2.3 - 2.35 Å
Structure data

PDB-4hyv:
Pyruvate kinase (PYK) from Trypanosoma brucei in the presence of Magnesium, PEP and F26BP
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-4hyw:
Pyruvate kinase (PYK) from Trypanosoma brucei in the presence of Magnesium and F26BP
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-PEP:
PHOSPHOENOLPYRUVATE

ChemComp-FDP:
2,6-di-O-phosphono-beta-D-fructofuranose

ChemComp-GOL:
GLYCEROL

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • trypanosoma brucei brucei (eukaryote)
KeywordsTRANSFERASE / Allosteric regulation / tetramer / Pyruvate Kinase / FRUCTOSE-2 / 6-DIPHOSPHATE binding / Phosphoenolpyruvate binding / cytosol

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