An Exceptional Variability in the Motor of Archaeal A1A0 ATPases: From Multimeric to Monomeric Rotors Comprising 6–13 Ion Binding Sites

@article{Mller2004AnEV,
  title={An Exceptional Variability in the Motor of Archaeal A1A0 ATPases: From Multimeric to Monomeric Rotors Comprising 6–13 Ion Binding Sites},
  author={Volker M{\"u}ller},
  journal={Journal of Bioenergetics and Biomembranes},
  year={2004},
  volume={36},
  pages={115-125}
}
  • V. Müller
  • Published 2004
  • Biology, Medicine
  • Journal of Bioenergetics and Biomembranes
The motor domain of A1A0 ATPases is composed of only two subunits, the stator subunit I and the rotor subunit c. Recent studies on the molecular biology of the A0 domains revealed the surprising finding that the gene encoding subunit c underwent several multiplication events leading to rotor subunits comprising 2, 3, or even 13 hairpin domains suggesting multimeric in different stoichiometry as well as monomeric rotors. The number of ion translocating groups per rotor ranges from 13 to 6… Expand

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