A common topology of proteins catalyzing ATP-triggered reactions.
A protein fold, six parallel beta strands surrounding the central alpha helix, is likely to be a common structure in protein families known to have a typical set of nucleotide binding consensus sequence 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 gamma-phosphate, is at the exit of the second beta strand. The fifth beta strand may be involved in propagation of conformational change triggered by ATP hydrolysis.
Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Yokohama, Japan.
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Yoshida
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Amano
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000595:Amino Acid Sequence; D001665:Binding Sites; D017124:Conserved Sequence; D018698:Glutamic Acid; D006868:Hydrolysis; D008969:Molecular Sequence Data; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
D011506:Proteins; D018698:Glutamic Acid; D000255:Adenosine Triphosphate