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Structure paper

TitleStructural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops.
Journal, issue, pagesStructure, Vol. 16, Page 1849-1859, Year 2008
Publish dateOct 16, 2008 (structure data deposition date)
AuthorsKato, M. / Wynn, R.M. / Chuang, J.L. / Tso, S.C. / Machius, M. / Li, J. / Chuang, D.T.
External linksStructure / PubMed:19081061
MethodsX-ray diffraction
Resolution1.979 - 3.011 Å
Structure data

PDB-3exe:
Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex
Method: X-RAY DIFFRACTION / Resolution: 1.979 Å

PDB-3exf:
Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex
Method: X-RAY DIFFRACTION / Resolution: 2.998 Å

PDB-3exg:
Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex
Method: X-RAY DIFFRACTION / Resolution: 3.011 Å

PDB-3exh:
Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex
Method: X-RAY DIFFRACTION / Resolution: 2.444 Å

PDB-3exi:
Crystal structure of the pyruvate dehydrogenase (E1p) component of human pyruvate dehydrogenase complex with the subunit-binding domain (SBD) of E2p, but SBD cannot be modeled into the electron density
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-TPP:
THIAMINE DIPHOSPHATE

ChemComp-GOL:
GLYCEROL

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-CL:
Unknown entry

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / heterotetramer; thiamine diphosphate-dependent enzyme; Disease mutation; Glycolysis; Leigh syndrome; Mitochondrion; Oxidoreductase; Phosphoprotein; Alternative splicing; Polymorphism; Pyruvate; Thiamine pyrophosphate; Transit peptide

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