Structural model of the ATP-binding domain of the F1-beta subunit based on analogy to the RecA protein.
In contrast to the previous topological model of the ATP binding domain of the F1-ATPase beta subunit based on analogies to those of ras p21 and adenylate kinase, a more consistent model can be constructed with the known structure of the recA protein as a reference. The secondary structure of the F1-ATPase beta subunit predicted from the primary structure agrees well with that of the recA protein. The topology includes a repetitive beta alpha c beta alpha beta alpha beta alpha beta structure where all beta strands are parallel and surround the central alpha c helix above which bound ATP is located. Several residues thought to be located at catalytic site as reported in genetic and chemical labeling work can be consistently positioned in this model.
Amano
T
T
Research Laboratory of Resources Utilization, R-1, Tokyo Institute of Technology, Yokohama, Japan.
Yoshida
M
M
Matsuo
Y
Y
Nishikawa
K
K
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000595:Amino Acid Sequence; D001665:Binding Sites; D008969:Molecular Sequence Data; D015689:Oncogene Protein p21(ras) / Q000737:chemistry; D017433:Protein Structure, Secondary; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism; D011938:Rec A Recombinases / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D014443:Tyrosine / Q000737:chemistry
D014443:Tyrosine; D000255:Adenosine Triphosphate; D011938:Rec A Recombinases; D006180:Proton-Translocating ATPases; D015689:Oncogene Protein p21(ras)