Mutations in the dimerization domain of the b subunit from the Escherichia coli ATP synthase. Deletions disrupt function but not enzyme assembly.

Abstract excerpt

The b subunit dimer of Escherichia coli ATP synthase serves essential roles as an assembly factor for the enzyme and as a stator during rotational catalysis. To investigate the functional importance of its coiled coil dimerization domain, a series of internal deletions including each individual residue between Lys-100 and Ala-105 (b(deltaK100)-b(deltaA105)), b(deltaK100-A103), and b(deltaK100-Q106) as well as a...

Topics

• Amino Acid Sequence
• Bacterial Proton-Translocating ATPases
• Base Sequence
• Cross-Linking Reagents
• Dimerization
• Escherichia coli
• Molecular Sequence Data
• Mutagenesis
• Mutagenesis, Site-Directed
• Mutation