Dimerization of bovine F1-ATPase by binding the inhibitor protein, IF1.

@article{Cabezn2000DimerizationOB,
  title={Dimerization of bovine F1-ATPase by binding the inhibitor protein, IF1.},
  author={Elena Cabez{\'o}n and Ignacio Arechaga and Philip Jonathan and Geraldine Butler and John E Walker},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 37},
  pages={28353-5}
}
In mitochondria, the hydrolytic activity of ATP synthase is regulated by a natural inhibitor protein, IF(1). The binding of IF(1) to ATP synthase depends on pH values, and below neutrality, IF(1) forms a stable complex with the enzyme. Bovine IF(1) has two oligomeric states, dimer and tetramer, depending on pH values. At pH 6.5, where it is active, IF(1) dimerizes by formation of an antiparallel alpha-helical coiled-coil in its C-terminal region. This arrangement places the inhibitory N… CONTINUE READING

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