The isolated H4-H5 cytoplasmic loop of Na,K-ATPase overexpressed in Escherichia coli retains its ability to bind ATP
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
9600254
DOI
10.1016/s0014-5793(98)00373-1
PII: S0014-5793(98)00373-1
Knihovny.cz E-resources
- MeSH
- Adenosine Triphosphate metabolism MeSH
- Cytoplasm enzymology MeSH
- Escherichia coli enzymology genetics MeSH
- Ethenoadenosine Triphosphate metabolism MeSH
- Genetic Vectors chemical synthesis MeSH
- Brain MeSH
- Mice MeSH
- Peptide Fragments genetics isolation & purification metabolism MeSH
- Recombinant Fusion Proteins biosynthesis isolation & purification metabolism MeSH
- Sodium-Potassium-Exchanging ATPase biosynthesis genetics metabolism MeSH
- Protein Structure, Tertiary MeSH
- Protein Binding genetics MeSH
- Binding Sites genetics MeSH
- Animals MeSH
- Check Tag
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Adenosine Triphosphate MeSH
- Ethenoadenosine Triphosphate MeSH
- Peptide Fragments MeSH
- Recombinant Fusion Proteins MeSH
- Sodium-Potassium-Exchanging ATPase MeSH
The H4-H5 loop of the alpha-subunit of mouse brain Na,K-ATPase was expressed and isolated from Escherichia coli cells. Using fluorescence analogues of ATP, this loop was shown to retain its capability to bind ATP. Isolation of a soluble H4-H5 loop with the native ATP binding site is a crucial step for detailed studies of the molecular mechanism of ATP binding and utilisation.
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