A common topology of proteins catalyzing ATP-triggered reactions

AbstractA protein fold, six parallel β strands surrounding the central α helix, is likely to be a common structure in protein families known to have a typical set of nucleotide binding consensus sequenced motifs A and B and to catalyze ATP-triggered reactions. According to this ATP-triggered protein fold, the conserved Glu (or Asp), which acts as a general base to activate a water molecule for an in-line attack of the γ-phosphate, is at the exit of the second β strand. The fifth β strand may be involved in propagation of conformational change triggered by ATP hydrolysis