Article
The nucleotide-binding domain of the Zn2+-transporting P-type ATPase from Escherichia coli carries a glycine motif that may be involved in binding of ATP.
The Biochemical journal - 1 Jan 2004
Okkeri Juha, Laakkonen Liisa, Haltia Tuomas
Abstract excerpt
In P-type ATPases, the nucleotide-binding (N) domain is located in the middle of the sequence which folds into the phosphorylation (P) domain. The N domain of ZntA, a Zn2+-translocating P-type ATPase from Escherichia coli, is approx. 13% identical with the N domain of sarcoplasmic reticulum Ca2+-ATPase. None of the Ca2+-ATPase residues involved in binding of ATP are found in ZntA. However, the sequence...
Topics
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Amino Acid Motifs
- Amino Acid Sequence
- Binding Sites
- Escherichia coli
- Glycine
- Histidine
- Kinetics
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Nucleotides
- Phosphorylation