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Structure of bacterial glucokinases
The structure of the bacterial glucokinase is unexpectedly similar to those of two ATP-dependent kinases, ribokinase and adenosine kinase and not to human glocokinase. Comparison based on three-dimensional structure revealed that several motifs important both in structure and function are conserved. The most important conservation is the binding site for the terminal and adjacent phosphate moieties. The overall structure of ADP-dependent glucokinase from T. litoralis (tlGK) complexed with ADP can be divided into large and small α/β domains, and the ADP molecule is buried in a shallow pocket in the large domain (shown white here). The ADP phosphate recognition loop is important for ADP binding and colored purple here. Ito S, Fushinobu S, Yoshioka I, Koga S, Matsuzawa H, Wakagi T. Structural basis for the ADP-specificity of a novel glucokinase from a hyperthermophilic archaeon Structure (2001) (PubMed) 1GC5 (PDB) |