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Structure paper

TitleStructural characterizations of glycerol kinase: unraveling phosphorylation-induced long-range activation
Journal, issue, pagesBiochemistry, Vol. 48, Page 346-356, Year 2009
Publish dateMay 21, 2008 (structure data deposition date)
AuthorsYeh, J.I. / Kettering, R. / Saxl, R. / Bourand, A. / Darbon, E. / Joly, N. / Briozzo, P. / Deutscher, J.
External linksBiochemistry / PubMed:19102629
MethodsX-ray diffraction
Resolution1.73 - 2.65 Å
Structure data

PDB-3d7e:
Enterococcus casseliflavus glycerol kinase mutant HIS232ALA complexed with glycerol
Method: X-RAY DIFFRACTION / Resolution: 2.03 Å

PDB-3flc:
Crystal structure of the His-tagged H232R mutant of glycerol kinase from Enterococcus casseliflavus with glycerol
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-3h3n:
Glycerol Kinase H232R with Glycerol
Method: X-RAY DIFFRACTION / Resolution: 1.73 Å

PDB-3h3o:
Glycerol Kinase H232R with Ethylene Glycol
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-3h45:
Glycerol Kinase H232E with Ethylene Glycol
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

PDB-3h46:
Glycerol Kinase H232E with Glycerol
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PO4:
PHOSPHATE ION

Source
  • enterococcus casseliflavus (bacteria)
KeywordsTRANSFERASE / KINASE / ATP-binding / Glycerol metabolism / Nucleotide-binding / Phosphoprotein / glycerol / ethylene glycol

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