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Structure paper

TitleCovalently Bound Substrate at the Regulatory Site of Yeast Pyruvate Decarboxylases Triggers Allosteric Enzyme Activation.
Journal, issue, pagesJ. Biol. Chem., Vol. 284, Page 12136-, Year 2009
Publish dateDec 14, 2007 (structure data deposition date)
AuthorsKutter, S. / Weiss, M.S. / Wille, G. / Golbik, R. / Spinka, M. / Konig, S.
External linksJ. Biol. Chem. / PubMed:19246454
MethodsX-ray diffraction
Resolution1.42 - 2.3 Å
Structure data

PDB-2vjy:
Pyruvate decarboxylase from Kluyveromyces lactis in complex with the substrate analogue methyl acetylphosphonate
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-2vk1:
Crystal structure of the Saccharomyces cerevisiae pyruvate decarboxylase variant D28A in complex with its substrate
Method: X-RAY DIFFRACTION / Resolution: 1.71 Å

PDB-2vk8:
Crystal structure of the Saccharomyces cerevisiae pyruvate decarboxylase variant E477Q in complex with its substrate
Method: X-RAY DIFFRACTION / Resolution: 1.42 Å

Chemicals

ChemComp-TPP:
THIAMINE DIPHOSPHATE

ChemComp-MG:
Unknown entry

ChemComp-ALK:
methoxy-[(1~{R})-1-oxidanylethyl]phosphinic acid

ChemComp-ALU:
METHYL HYDROGEN (S)-ACETYLPHOSPHONATE

ChemComp-HOH:
WATER

ChemComp-PYR:
PYRUVIC ACID

ChemComp-2OP:
(2S)-2-HYDROXYPROPANOIC ACID

Source
  • kluyveromyces lactis (yeast)
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsLYASE / METAL-BINDING / DECARBOXYLASE / DIMER OF DIMERS / METHYLACETYLPHOSPHONATE / METHYL ACETYLPHOSPHONATE / SUBSTRATE ACTIVATION / THIAMINE DIPHOSPHATE / THIAMINE PYROPHOSPHATE / ASYMMETRIC ACTIVE SITES / MAP / PYRUVATE / MAGNESIUM / FLAVOPROTEIN / PHENYLALANINE CATABOLISM / TRYPTOPHAN CATABOLISM / PHOSPHORYLATION / ALLOSTERIC ENZYME / TDP / TPP / NUCLEUS / CYTOPLASM / BRANCHED-CHAIN AMINO ACID CATABOLISM / ACETYLATION

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