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Structure paper

TitleCrystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction.
Journal, issue, pagesNat. Struct. Mol. Biol., Vol. 15, Page 295-302, Year 2008
Publish dateNov 26, 2007 (structure data deposition date)
AuthorsXiang, S. / Tong, L.
External linksNat. Struct. Mol. Biol. / PubMed:18297087
MethodsX-ray diffraction
Resolution2.8 - 3 Å
Structure data

PDB-3bg3:
Crystal Structure of Human Pyruvate Carboxylase (missing the biotin carboxylase domain at the N-terminus)
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-3bg5:
Crystal Structure of Staphylococcus Aureus Pyruvate Carboxylase
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-3bg9:
Crystal Structure of Human Pyruvate Carboxylase (missing the biotin carboxylase domain at the N-terminus) F1077A Mutant
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-PYR:
PYRUVIC ACID

ChemComp-BTI:
5-(HEXAHYDRO-2-OXO-1H-THIENO[3,4-D]IMIDAZOL-6-YL)PENTANAL

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Source
  • homo sapiens (human)
  • staphylococcus aureus (bacteria)
KeywordsLIGASE / TIM barrel / ATP-binding / Biotin / Disease mutation / Gluconeogenesis / Lipid synthesis / Manganese / Mitochondrion / Multifunctional enzyme / Nucleotide-binding / Phosphoprotein / Transit peptide / Pyruvate

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