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Structure paper

TitleSwiveling domain mechanism in pyruvate phosphate dikinase.
Journal, issue, pagesBiochemistry, Vol. 46, Page 14845-14853, Year 2007
Publish dateSep 10, 2007 (structure data deposition date)
AuthorsLim, K. / Read, R.J. / Chen, C.C. / Tempczyk, A. / Wei, M. / Ye, D. / Wu, C. / Dunaway-Mariano, D. / Herzberg, O.
External linksBiochemistry / PubMed:18052212
MethodsX-ray diffraction
Resolution3 - 3.6 Å
Structure data

PDB-2r82:
Pyruvate phosphate dikinase (PPDK) triple mutant R219E/E271R/S262D adapts a second conformational state
Method: X-RAY DIFFRACTION / Resolution: 3.6 Å

PDB-9pzl:
Pyruvate phosphate dikinase in complex with AMP-PNP and sulfate ions
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • clostridium symbiosum (bacteria)
KeywordsTRANSFERASE / phosphotransferase / conformational transition / swiveling domain / remote active sites / ATP-binding / Kinase / Magnesium / Metal-binding / Nucleotide-binding / Phosphorylation / PEP BINDING DIKINASE

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