Molecule of the Month
December 2003
Crystal Structure of the Citrobacter freundii Dihydroxyacetone Kinase Reveals an Eight-stranded a-Helical Barrel ATP-binding Domain

This is the nucleotide binding domain of the dihydroxyacetone kinase of Citrobacter freundii complexed with AMPPNP (red) and a phospholipid (green). Met and Phe (yellow) separate the nucleotide-binding depression from the lipid-binding pocket of the eight-helix barrel. Homologous domains occur in the PTS-dependent kinase of E.coli and proteins associated with various transcription factors.

This work was carried out in the group of Prof. Bernhard Erni.

References:

  • C. Siebold, I. Arnold, L. F. Garcia-Alles, U. Baumann, B. Erni;
    "Crystal Structure of the Citrobacter freundii Dihydroxyacetone Kinase Reveals an Eight-stranded a-Helical Barrel ATP-binding Domain"
    J. Biol. Chem., 278, 48236-48244, (2003); doi:10.1074/jbc.M305942200.