Structural model of the ATP‐binding domain of the F1‐β subunit based on analogy to the RecA protein

FEBS Letters

Matsuo, Yo¹  Amano, Toyoki²  Nishikawa, Ken¹  Yoshida, Masasuke² 

[1] Protein Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka 565, Japan;Research Laboratory of Resources Utilization, R-1, Tokyo Institute of Technology, Nagatsuta 4259, Yokohama 227, Japan

关键词: F1-ATPase;    ATP binding domain;    ATP binding motif;    RecA;    Dicyclohexylcarbodiimide;    TF1;    F1-ATPase from a thermophilic Bacillus strain PS3;    Nbf-Cl;    7-chloro-4-nitrobenzofrazan;   

DOI  :  10.1016/0014-5793(94)00796-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In contrast to the previous topological model of the ATP binding domain of the F₁-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 F₁-ATPase β subunit predicted from the primary structure agrees well with that of the recA protein. The topology includes a repetitive βα_Cβαβαβαβ 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.

【 授权许可】

Unknown