Article
Roles of the beta subunit hinge domain in ATP synthase F(1) sector: hydrophobic network formed by introduced betaPhe174 inhibits subunit rotation.
Biochemical and biophysical research communications - 30 Apr 2010
Nakanishi-Matsui Mayumi, Kashiwagi Sachiko, Kojima Masaki, Nonaka Takamasa, Futai Masamitsu
Abstract excerpt
The ATP synthase beta subunit hinge domain (betaPhe148 approximately betaGly186, P-loop/alpha-helixB/loop/beta-sheet4, Escherichia coli residue numbering) dramatically changes in conformation upon nucleotide binding. We previously reported that F(1) with the betaSer174 to Phe mutation in the domain lowered the gamma subunit rotation speed, and thus decreased the ATPase activity [M. Nakanishi-Matsui, S. Kashiwagi,...
Topics
- ATP Synthetase Complexes
- Amino Acid Substitution
- Escherichia coli
- Escherichia coli Proteins
- Hydrophobic and Hydrophilic Interactions
- Membrane Proteins
- Mutation
- Phenylalanine
- Protein Structure, Secondary
- Protein Structure, Tertiary
- Protein Subunits
- Rotation
- Transcription Factors