Genetic evidence for two sequentially occupied K+ binding sites in the Kdp transport ATPase.

Abstract excerpt

Substrate binding sites in Kdp, a P-type ATPase of Escherichia coli, were identified by the isolation and characterization of mutants with reduced affinity for K+, its cation substrate. Most of the mutants have an altered KdpA subunit, a hydrophobic subunit not found in other P-type ATPases. Topo...

Topics

• Adenosine Triphosphatases
• Adenosine Triphosphate
• Amino Acid Sequence
• Binding Sites
• Calcium-Transporting ATPases
• Carrier Proteins
• Cation Transport Proteins
• Escherichia coli Proteins
• Molecular Sequence Data
• Mutation
• Potassium