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Structure paper

TitlePyruvate kinases have an intrinsic and conserved decarboxylase activity.
Journal, issue, pagesBiochem. J., Vol. 458, Page 301-311, Year 2014
Publish dateApr 24, 2013 (structure data deposition date)
AuthorsZhong, W. / Morgan, H.P. / Nowicki, M.W. / McNae, I.W. / Yuan, M. / Bella, J. / Michels, P.A. / Fothergill-Gilmore, L.A. / Walkinshaw, M.D.
External linksBiochem. J. / PubMed:24328825
MethodsX-ray diffraction
Resolution1.95 - 2.5 Å
Structure data

PDB-4kct:
Pyruvate kinase (PYK) from Trypanosoma brucei soaked with Oxaloacetate
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-4kcu:
Pyruvate kinase (PYK) from Trypanosoma brucei soaked with D-Malate
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

PDB-4kcv:
Pyruvate kinase (PYK) from Trypanosoma brucei soaked with 2-oxoglutaric acid
Method: X-RAY DIFFRACTION / Resolution: 2.18 Å

PDB-4kcw:
Pyruvate kinase (PYK) from Trypanosoma brucei soaked with oxalate
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-PYR:
PYRUVIC ACID

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

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-MLT:
D-MALATE

ChemComp-AKG:
2-OXOGLUTARIC ACID

ChemComp-OXL:
OXALATE ION

Source
  • trypanosoma brucei brucei (eukaryote)
KeywordsTRANSFERASE / pyruvate kinase / decarboxylase

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