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TitleStructural Analysis of the Bacterial HPr Kinase/Phosphorylase V267F Mutant Gives Insights into the Allosteric Regulation Mechanism of This Bifunctional Enzyme.
Journal, issue, pagesJ. Biol. Chem., Vol. 282, Page 34952-34957, Year 2007
Publish dateJul 16, 2007 (structure data deposition date)
AuthorsChaptal, V. / Vincent, F. / Gueguen-Chaignon, V. / Monedero, V. / Poncet, S. / Deutscher, J. / Nessler, S. / Morera, S.
External linksJ. Biol. Chem. / PubMed:17878158
MethodsX-ray diffraction
Resolution2.6 Å
Structure data

PDB-2qmh:
structure of V267F mutant HprK/P
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • lactobacillus casei (bacteria)
KeywordsTRANSFERASE / V267F mutation / ATP-binding / Carbohydrate metabolism / Kinase / Magnesium / Metal-binding / Multifunctional enzyme / Nucleotide-binding / Serine/threonine-protein kinase / METAL BINDING PROTEIN

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