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.
Yoshida
M
M
Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Yokohama, Japan.
Amano
T
T
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