Article
Mutations on the N-terminal edge of the DELSEED loop in either the α or β subunit of the mitochondrial F1-ATPase enhance ATP hydrolysis in the absence of the central γ rotor.
Eukaryotic cell - 1 Nov 2013
La Thuy, Clark-Walker George Desmond, Wang Xiaowen, Wilkens Stephan, Chen Xin Jie
Abstract excerpt
F(1)-ATPase is a rotary molecular machine with a subunit stoichiometry of α(3)β(3)γ(1)δ(1)ε(1). It has a robust ATP-hydrolyzing activity due to effective cooperativity between the three catalytic sites. It is believed that the central γ rotor dictates the sequential conformational changes to the catalytic sites in the α(3)β(3) core to achieve cooperativity. However, recent studies of the thermophilic Bacillus PS3...
Topics
- Adenosine Triphosphate
- Amino Acid Motifs
- Amino Acid Sequence
- Catalytic Domain
- Fungal Proteins
- Hydrolysis
- Kluyveromyces
- Mitochondrial Proton-Translocating ATPases
- Molecular Sequence Data
- Mutation
- Protein Subunits