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Structural model of the ATP‐binding domain of the F 1 ‐β subunit based on analogy to the RecA protein
Author(s) -
Amano Toyoki,
Yoshida Masasuke,
Matsuo Yo,
Nishikawa Ken
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00796-9
Subject(s) - analogy , protein subunit , domain (mathematical analysis) , chemistry , biophysics , computational biology , biochemistry , biology , mathematics , philosophy , gene , mathematical analysis , linguistics
In contrast to the previous topological model of the ATP binding domain of the F 1 ‐ATPase β 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 F 1 ‐ATPase β subunit predicted from the primary structure agrees well with that of the recA protein. The topology includes a repetitive βα C βαβαβαβ structure where all β strands are parallel and surround the central α 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.